ライフサイエンスコーパス: misfolding

1 fferent as starvation, infection, or protein misfolding.

2 ion of the proteostasis network upon protein misfolding.

3 l, associated with protein modifications and misfolding.

4 enetic disease associated with wild-type TTR misfolding.

5 ld cotranslationally to minimize interdomain misfolding.

6 gomers form during the early steps of TDP-43 misfolding.

7 ce for understanding disease-related protein misfolding.

8 odeling suggests that they result in protein misfolding.

9 protein revealed no evidence of significant misfolding.

10 oluble under conditions that promote protein misfolding.

11 ns and the deleterious consequences of their misfolding.

12 ps to avoid otherwise prevalent inter-domain misfolding.

13 g protein homeostasis and preventing protein misfolding.

14 nd neurobiological defects caused by protein misfolding.

15 anism that chaperones may exploit to prevent misfolding.

16 n, possibly due to increased cotranslational misfolding.

17 d by poor solubility, low yield, and protein misfolding.

18 ism of this novel tactic of ligand-regulated misfolding.

19 nformation, with no evidence for large-scale misfolding.

20 ns and the end product of pathologic protein misfolding.

21 lt in an increase in toxicity due to protein misfolding.

22 ases associated with cell stress and protein misfolding.

23 cally, thereby potentiating slow folding and misfolding.

24 nt molecular chaperone that inhibits protein misfolding.

25 assemblies that propagate by seeded protein misfolding.

26 in which he developed strategies to prevent misfolding.

27 nderappreciated factor in initiating protein misfolding.

28 neurodegenerative diseases caused by protein misfolding.

29 in the GAF-B domain of PDE10A induce PDE10A misfolding, a common pathological phenotype in many neur

30 's disease (AD) and other tauopathies is the misfolding, aggregation and cerebral accumulation of tau

31 teins no longer keeps up with depletion from misfolding, aggregation, and damage.

32 isease, it is now well-established that upon misfolding, alphasyn acquires pathogenic properties, suc

33 Extending our findings, we show that misfolding also occurs for IL-23alpha, another IL-12 fam

34 hypotheses and provided evidence for protein misfolding and aberrant target recognition as the underl

35 When these processes are not regulated, misfolding and accumulation of aberrant proteins can occ

36 The misfolding and accumulation of alpha-synuclein (alphaS)

37 ive diseases characterized by dysregulation, misfolding and accumulation of specific proteins in the

38 This substitution is associated with misfolding and accumulation of ZAAT in the endoplasmic r

39 ooked role in the propagation of tau protein misfolding and AD pathogenesis, providing a new conceptu

40 ted in the initiation and progression of tau misfolding and aggregation are largely unclear.

41 ults demonstrate that CLR01 can inhibit SOD1 misfolding and aggregation both in vitro and in vivo, bu

42 homeostasis occurring as a result of protein misfolding and aggregation contributes to the pathogenes

43 the UPR is not induced as a response to tau misfolding and aggregation despite clear evidence for pr

44 These misfolding and aggregation events are associated with th

45 s known about the factors that cause protein misfolding and aggregation in metazoans.

46 -loop, a characteristic which contributes to misfolding and aggregation in neurodegenerative disease.

47 Cells respond to protein misfolding and aggregation in the cytosol by adjusting g

48 alpha-Synuclein misfolding and aggregation is a hallmark in Parkinson's

49 oxicity associated with beta-amyloid (Abeta) misfolding and aggregation is a promising therapeutic st

50 Protein misfolding and aggregation is increasingly being recogni

51 Protein misfolding and aggregation is the hallmark of numerous h

52 The misfolding and aggregation of alpha-synuclein (alphasyn)

53 rative diseases that are associated with the misfolding and aggregation of alpha-synuclein, including

54 rodegenerative diseases are characterized by misfolding and aggregation of an expanded polyglutamine

55 t pancreatic IAPP aggregates can promote the misfolding and aggregation of endogenous IAPP in islet c

56 Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo

57 This expansion leads to misfolding and aggregation of mutant ataxin-3 (ATXN3) an

58 front line of protection from stress-induced misfolding and aggregation of polypeptides in most organ

59 The misfolding and aggregation of proteins leading to amyloi

60 Heat stress induces misfolding and aggregation of proteins unless they are g

61 olded aggregate or 'seed' promotes the rapid misfolding and aggregation of the native protein.

62 ressive neurodegenerative disorder caused by misfolding and aggregation of the prion protein (PrP), a

63 alpha-Synuclein misfolding and aggregation plays a major role in the pat

64 ular structure of great interest because its misfolding and aggregation, along with changes in the se

65 tive serpin fold renders them susceptible to misfolding and aggregation, and underlies misfolding dis

66 athogenic mechanisms include alpha-synuclein misfolding and aggregation, mitochondrial dysfunction, i

67 ase (SOD1) upon translation promotes protein misfolding and aggregation, which has been linked to ALS

68 nderstand the principles that govern protein misfolding and aggregation, which is a highly complex pr

69 ns, being a key aspect in pathogenic protein misfolding and aggregation.

70 passing to naive cells in which it templates misfolding and aggregation.

71 sical properties of proteins associated with misfolding and aggregation.

72 P23H-1 rat retina, suggesting enhanced P23H misfolding and aggregation.

73 ostasis (proteostasis), resulting in protein misfolding and aggregation.

74 teostasis, by mitigating the risk of protein misfolding and aggregation.

75 e diseases characterized by aberrant protein misfolding and aggregation.

76 erse prokaryotic and eukaryotic cells in tau misfolding and aggregation.

77 mains have shown an increased propensity for misfolding and aggregation.

78 , particularly early events that trigger the misfolding and assembly of the otherwise soluble and sta

79 ich may limit the deleterious effects of RNH misfolding and assist in folding fidelity.

80 F) was shown to directly inhibit mutant SOD1 misfolding and binding to intracellular membranes.

81 ssociated with hyperglycemia-induced protein misfolding and Caspase-8-induced programmed cell death.

82 pansion in the Htt protein, resulting in Htt misfolding and cell death.

83 ng pyrin and the actin cytoskeleton, protein misfolding and cellular stress, NF-kappaB dysregulation

84 ing network to study the folding, unfolding, misfolding and conformational plasticity of the high-eff

85 hERG) potassium channel, many of which cause misfolding and degradation at the endoplasmic reticulum

86 tion and biological activity of IL-12 versus misfolding and degradation of IL-12alpha.

87 Membrane proteins are prone to misfolding and degradation within the cell, yet the natu

88 uggested that mutant GCase protein undergoes misfolding and degradation, and therefore, stabilization

89 e expression of proteins to minimize protein misfolding and denaturation.

90 The clear link between protein misfolding and disease highlights the need to better und

91 sense variants in EHMT1 that lead to protein misfolding and disrupted histone mark binding can lead t

92 nthesis at night, thereby preventing protein misfolding and ER stress.

93 This observation suggested that the misfolding and functional defects caused by the E217G mu

94 Given the many linkages between MP misfolding and human disease, we also examine some of th

95 gle cause of RP in the USA, causes rhodopsin misfolding and induction of the unfolded protein respons

96 identified a compound that inhibits alphaSyn misfolding and is neuroprotective, multiple compounds th

97 , resulting in Phe-508 deletion, causes CFTR misfolding and its premature degradation.

98 y protecting nascent polypeptide chains from misfolding and maintain translational fidelity by involv

99 ve slowly because of selection against toxic misfolding and misinteractions, linking their rate of ev

100 MT1A leads to a disproportionate increase in misfolding and mistrafficking of PMP22, which is likely

101 ature reporting a role of lipids in alphasyn misfolding and neurotoxicity in various synucleinopathy

102 roteasomal responses are due to AgDD protein misfolding and not to the presence of detergent-insolubl

103 mbled ribosomal proteins are highly prone to misfolding and often require dedicated chaperones to pre

104 Protein misfolding and overloaded proteostasis networks underlie

105 verview of current methods to assess protein misfolding and pathogenicity both in vitro and in vivo.

106 e protease inhibitor alpha(1)-antitrypsin to misfolding and polymerisation within hepatocytes, causin

107 anges the protein structure and leads to its misfolding and polymerization, which cause endoplasmic r

108 ctance regulator (CFTR) anion channel causes misfolding and premature degradation.

109 oxic due to their strong ability to seed tau misfolding and propagate the pathology seen across diffe

110 These fibrils may induce further alphasyn misfolding and propagation of pathologic fibrils in a pr

111 ids drive tau-membrane association, inducing misfolding and self-assembly of the disordered tau into

112 on the molecular factors involved in protein misfolding and the development of ultrasensitive methods

113 The mechanisms that produce alphasyn misfolding and the molecular events underlying the neuro

114 standing of the mechanism of alpha-synuclein misfolding and the structures of the aggregates that are

115 Co-expression of its beta subunit inhibits misfolding and thus allows secretion of biologically act

116 s qualitatively different aspects of protein misfolding and toxicity via different quaternary structu

117 ion, we characterized its effect on alphaSyn misfolding and transmission in experimental models of Pa

118 ts shed new light on the roles of NAs in PrP misfolding and TSEs.

119 er potential triggers of the alpha-synuclein misfolding and why the aggregates escape cellular degrad

120 toxic effects of mutant protein expression, misfolding, and aggregation.

121 rom neurodegeneration underpinned by protein misfolding, and enhanced Hsp104 variants strongly counte

122 ent hypothesis is that hyperphosphorylation, misfolding, and fibrillization of tau impair synaptic pl

123 ne destination and are prone to aggregation, misfolding, and mislocalization during this process.

124 ular perspective on cotranslational folding, misfolding, and the impact of translation speed on these

125 t make rabbit recombinant PrP susceptible to misfolding, and using these, protease-resistant misfolde

126 ms underlying the pathological properties of misfolding- and aggregation-prone proteins remain a chal

127 f cellular compartments to cytosolic protein misfolding are less clear.

128 established paradigms for how MP folding and misfolding are linked to the molecular etiologies of a v

129 of human disease, and therapies that target misfolding are transforming the clinical care of cystic

130 eric VWF and provides strong support for VWF misfolding as a result of some, but not all, type 2 VWD

131 es showed that this variant leads to protein misfolding as well as less effective tail-anchored prote

132 olds potential for the management of protein misfolding-associated diseases.

133 rescence studies show that HNG inhibits IAPP misfolding at highly substoichiometric concentrations.

134 lating SAA is protected from proteolysis and misfolding by binding to plasma high-density lipoprotein

135 proposed to exert protective effects against misfolding by interfering with eIF2alpha-P dephosphoryla

136 nslation and proper protein folding, whereas misfolding can lead to aggregation and disease.

137 chaperones and protein folding facilitators, misfolding can occur quite frequently.

138 Protein misfolding caused by inherited mutations leads to loss o

139 Rhodopsin misfolding caused by the P23H mutation is a major cause

140 Protein misfolding causes a wide spectrum of human disease, and

141 ative disorder caused by prion protein (PrP) misfolding, clinically recognized by cognitive and motor

142 ve bacteria results in a more pronounced tau misfolding compared to eukaryotic DNA.

143 rol of dNTPs improves fitness during protein misfolding conditions.

144 Here, we optimized the protein misfolding cyclic amplification (PMCA) assay for highly

145 ensitivity and specificity using the Protein Misfolding Cyclic Amplification (PMCA) assay.

146 f prion seeding activity in vitro by protein misfolding cyclic amplification (PMCA) demonstrated that

147 )) has recently been demonstrated by protein misfolding cyclic amplification (PMCA) in urine of patie

148 Protein misfolding cyclic amplification (PMCA) is a technique th

149 Here we show the utility of the Protein Misfolding Cyclic Amplification (PMCA) technology as a s

150 munosorbent assay to measure NFL and protein misfolding cyclic amplification (PMCA) to detect alphaSy

151 and in vitro templating activity by protein misfolding cyclic amplification (PMCA) were studied.

152 d a prion conversion in vitro assay, protein misfolding cyclic amplification (PMCA), by using experim

153 sceptibility to PrP(Sc) propagation, protein misfolding cyclic amplification (PMCA), which mimics PrP

154 We further demonstrated protein misfolding cyclic amplification (PMCA)-competent prions

155 ing-induced conversion (RT-QuIC) and protein misfolding cyclic amplification (PMCA).

156 here we report ultrasensitive serial protein misfolding cyclic amplification (sPMCA) and real-time qu

157 s to monitor prion replication (i.e. protein misfolding cyclic amplification and cellular and animal

158 An adapted Protein Misfolding Cyclic Amplification methodology based on the

159 Horse prions produced in vitro by protein misfolding cyclic amplification of mouse prions using ho

160 ed control PrP(Sc) from PrP(C) using protein misfolding cyclic amplification with beads (PMCAb), and

161 y, conformation stability assay, and protein-misfolding cyclic amplification, we monitored the confor

162 id light-chain (LC) amyloidosis is a protein misfolding disease in which the aggregation of an overex

163 amyloidosis is a worldwide occurring protein misfolding disease of humans and animals.

164 nderstand the impact of epigenetics on human misfolding disease, we apply Gaussian-process regression

165 tanding the role of the epigenome in protein-misfolding diseases remains a challenge in light of gene

166 to misfolding and aggregation, and underlies misfolding diseases such as alpha(1)-antitrypsin deficie

167 ve significant benefit in correcting protein-misfolding diseases that occur in response to both famil

168 ing many neurodegenerative diseases, protein misfolding diseases, diabetes, ischemic disorders, and c

169 rm encephalopathies (TSEs) and other protein misfolding diseases, TSEs can be used to understand othe

170 fect that might also extend to other protein-misfolding diseases.

171 r homeostasis can be deteriorated in protein misfolding diseases.

172 pathologic states that are viewed as protein-misfolding diseases.

173 to development into therapeutics for protein-misfolding diseases.

174 g target for modifying the course of protein misfolding diseases.

175 Amyloids are implicated in many protein misfolding diseases.

176 Huntington's disease (HD) and other protein misfolding diseases.

177 to improve protein function in other protein misfolding diseases.

178 al of toxic proteins in a variety of protein misfolding diseases.

179 nt of potential therapeutics against protein-misfolding diseases.

180 tic interventions designed to combat protein misfolding diseases.

181 Both diseases are considered protein misfolding disorders associated with the accumulation of

182 ents for prion diseases and possibly protein misfolding disorders involving prion-like mechanisms.

183 rotein A1 (HtrA1) is associated with protein-misfolding disorders such as Alzheimer's disease and tra

184 pproach to the targeted treatment of protein misfolding disorders, wherein the stabilisation of disea

185 cretory pathway is disrupted in many protein misfolding disorders.

186 ection, monitoring and treatment of multiple misfolding disorders.

187 has important implications for human protein misfolding disorders.

188 pathies that are collectively termed protein misfolding disorders.

189 2D and AD, two of the most prevalent protein misfolding disorders.

190 Misfolding during biosynthesis in the ER activates the u

191 ue to a toxic gain-of-function intracellular misfolding event involving a mutated myocilin olfactomed

192 essive neurodegenerative disorders caused by misfolding followed by aggregation and accumulation of p

193 the immediate functional consequence of tau misfolding for the individual neuron is not well underst

194 mechanisms underlying the link among genome misfolding, genome dysregulation, and aberrant cellular

195 Proteins begin to fold in the ribosome, and misfolding has pathological consequences.

196 rRNA misfolding impairs the formation of 80S-like ribosomes,

197 oreceptor degeneration instigated by protein misfolding in a mouse model of retinopathy.

198 ology spreads between neurons and propagates misfolding in a prion-like manner throughout connected n

199 Moreover, proAVP misfolding in hereditary central diabetes insipidus like

200 hysiopathological mechanisms with proinsulin misfolding in hereditary diabetes mellitus of youth.

201 viously observed classic evidence of protein misfolding in mutations with severe phenotypes: differen

202 (PAN) to alleviate the toxicity from protein misfolding in neurodegenerative disease.

203 sign as well as defining the role of protein misfolding in neurodegenerative disorders.

204 xC57BL/6 F1 thymocytes revealed that genomic misfolding in NOD mice is mediated in cis.

205 ng our understanding on the possible role of misfolding in some ferritin-related pathologies and posi

206 nsitive antibody, TNT2, to determine whether misfolding in the amino terminus (ie, PAD exposure) occu

207 tasis networks mediate MP folding and manage misfolding in the cell.

208 tion (OxPhos) inhibitors and that ER protein misfolding increases ATP uptake from mitochondria into t

209 ally linked to cellular prion protein (PrPC) misfolding into abnormal conformers (PrPSc), with PrPSc

210 the prion protein (PrP(C)) influences PrP(C) misfolding into the disease-associated isoform, PrP(res)

211 Rhodopsin mutation and misfolding is a common cause of autosomal dominant retin

212 Protein misfolding is a common hypothesis underlying the develop

213 Protein misfolding is a key pathological event in neurodegenerat

214 Protein misfolding is a recurring phenomenon that cells must man

215 Misfolding is believed to be mediated by both the N- and

216 n emerging model in which genome folding and misfolding is critically linked to the onset and progres

217 lement (TAR) DNA-binding protein 43 (TDP-43) misfolding is implicated in several neurodegenerative di

218 stress, but how they help counteract protein misfolding is incompletely understood.

219 , despite the general knowledge that protein misfolding is intimately associated with dysfunction and

220 Protein misfolding is linked to a rapidly expanding list of huma

221 ed aggregates to an "acceptor cell" in which misfolding is propagated by conversion of the normal pro

222 Protein misfolding is toxic to cells and is believed to underlie

223 experimental strategy to study site-specific misfolding kinetics during aggregation, by effectively s

224 MYOC mutations result in protein misfolding, leading to endoplasmic reticulum (ER) stress

225 plays a significant role in SOD1 folding and misfolding mechanisms and strengthen the hypothesis that

226 Finally, we have found that GGPP-regulated misfolding occurred in detergent-solubilized Hmg2, a fea

227 This misfolding occurs via a transiently populated intermedia

228 Once misfolding occurs, the pathogenic isoform polymerizes in

229 , where one aggregated protein templates the misfolding of a heterologous protein, is one mechanism p

230 (PD) is associated with the aggregation and misfolding of alpha-syn in dopaminergic neurons.

231 Here, we show that misfolding of ALS-linked SOD1 mutants and wild-type (wt)

232 In vitro, the compounds induce misfolding of chromatin fibre and block the binding of t

233 adation of Hmg2 and required for mallosteric misfolding of GGPP as studied by in vitro limited proteo

234 erol pathway intermediate GGPP, which causes misfolding of Hmg2, leading to degradation by the HRD pa

235 line current perspectives on the folding and misfolding of integral MPs as well as the mechanisms of

236 f prolines is important for the activity and misfolding of intrinsically disordered proteins.

237 small humanin-like peptide 2 (SHLP2), on the misfolding of islet amyloid polypeptide (IAPP), a critic

238 at protects TMDs during assembly to minimize misfolding of multi-spanning membrane proteins and maint

239 Misfolding of mutant FUS is implicated in this process,

240 Misfolding of nascent Tpi1 in response to both cadmium a

241 shock response is triggered by heat-induced misfolding of newly synthesized polypeptides, and so has

242 The mistargeting or misfolding of PM proteins likely exposes these lysines o

243 a neurodegenerative disease associated with misfolding of protein tau, indicating that sCJD might sh

244 The misfolding of proteins and their accumulation in extrace

245 derstanding of diseases that result from the misfolding of proteins including diabetes type II, Alzhe

246 , we hypothesized that hsp60 mutations cause misfolding of proteins that are critical for aerobic res

247 gen species, protein chaperones that prevent misfolding of proteins, and proteases that degrade toxic

248 Misfolding of tau proteins into prions and their propaga

249 e rare, neurological disorders caused by the misfolding of the cellular prion protein (PrP(C)) into c

250 ive disorders in human and animals caused by misfolding of the cellular prion protein (PrP(C)) into t

251 Misfolding of the microtubule-binding protein tau into f

252 llagen, which increase ER stress by inducing misfolding of the mutant protein and subsequently disrup

253 fatal neurodegenerative disorders caused by misfolding of the normal prion protein into an infectiou

254 Introducing the mutation does not cause misfolding of the SH3 domains, but abolishes the interac

255 Misfolding of translated proteins occurs in all domains

256 ymes resulting in improper glycosylation and misfolding of viral glycoproteins.

257 Misfolding, oligomerization and accumulation of the huma

258 ng gene transcription in response to protein misfolding, oncogenic cell proliferation, and other envi

259 the functional relationship between protein misfolding or aggregation and the cellular proteostasis

260 provide a chaperone-like activity to prevent misfolding or aggregation as the preprotein traverses th

261 have the proteins they need while minimizing misfolding or aggregation events that are hallmarks of a

262 mation by protecting the native protein from misfolding or by targeting it for degradation, but no va

263 that lacked both chaperones, perhaps due to misfolding or instability.

264 tation is not associated with either protein misfolding or loss of function.

265 We propose that the E46K misfolding pathway avoids electrostatic repulsion betwee

266 werful approaches to dissect the complicated misfolding pathways of protein aggregation.

267 y while inhibiting further transitions along misfolding pathways.

268 chaperone trigger factor reduce inter-domain misfolding, permitting folding of the N-terminal G-domai

269 Cell-to-cell transmission of misfolding-prone alpha-synuclein (alpha-Syn) has emerged

270 predictions, we find that rapid synthesis of misfolding-prone nascent-chain segments increases the fr

271 ed to compute the folding pathways of large, misfolding-prone proteins that lie beyond the reach of e

272 Here we show that the underlying protein misfolding propagates rapidly between individual neurons

273 h, but the relationships between initial tau misfolding, propagation across connected neurons and cyt

274 tions in rabbit PrP and accurate analysis of misfolding propensities.

275 l folding using superhelicases shows reduced misfolding propensity and allowed a folding pathway diff

276 sps bind to early-unfolding intermediates of misfolding proteins in an ATP-independent manner and seq

277 tense scrutiny however, the mechanism of the misfolding reaction remains unclear.

278 The early stages of protein misfolding remain incompletely understood, as most mamma

279 nism is that ELANE mutations promote protein misfolding, resulting in endoplasmic reticulum stress an

280 the T415N variant causes significant protein misfolding, resulting in low protein expression, cellula

281 e data suggest that improving the traffic of misfolding rhodopsin mutants is unlikely to be a practic

282 dence supports transcellular transfer of tau misfolding (seeding) as the mechanism of spread within a

283 t NAC can protect astrocytes against protein misfolding stress (proteotoxicity), the hallmark of neur

284 ortant for cells to survive ER-based protein misfolding stress.

285 ino acid residue substitutions increased the misfolding susceptibility of rabbit PrP.IMPORTANCE Prion

286 Cdc5p and cohesin prevent condensin from misfolding the RDN into an irreversibly decondensed stat

287 ro due to their capacity towards seeding tau misfolding, thereby propagating the tau pathology seen a

288 ll reveal promising agents to combat protein misfolding toxicity in neurodegenerative disease.

289 neurodegenerative disease-associated protein misfolding toxicity in yeast, Caenorhabditis elegans, an

290 morbidities, such as chronic stress, protein misfolding, traumatic brain injury or other pathological

291 Protein misfolding underlies many neurodegenerative diseases inc

292 Protein misfolding underlies the pathology of a large number of

293 Here, we introduce a protocol to incorporate misfolding using the functional forms of publicly availa

294 GGPP-dependent misfolding was still extant but occurred at a much slowe

295 by binding of a small-molecule inhibitor of misfolding we conclude that they arise from rapid exchan

296 swapping is a potential source of transient misfolding, we demonstrate that such a kinetic trap reta

297 rget misfolded amyloid seeds to inhibit IAPP misfolding which, along with direct anti-apoptotic activ

298 Point mutations in SLC6 transporters cause misfolding, which can be remedied by pharmacochaperones.

299 owers the energy barrier for alpha-synuclein misfolding, while isomerase-binding to a separate, disea

300 pe of conformational disorder due to protein misfolding with consequent aberrant intermolecular prote