ライフサイエンスコーパス: misfolding

1 oluble under conditions that promote protein misfolding.

2 cally, thereby potentiating slow folding and misfolding.

3 degradation in the knock-in mouse RPE due to misfolding.

4 educe intercellular propagation of alpha-syn misfolding.

5 d unveil new targets for diseases of protein misfolding.

6 g protein homeostasis and preventing protein misfolding.

7 lded form and 2) any loss of function due to misfolding.

8 ession of misfolded proteins, induce protein misfolding.

9 r this delicate balance between function and misfolding.

10 vent their aggregation, premature folding or misfolding.

11 major amyloid "hot spot" can trigger protein misfolding.

12 crease protein stability and trigger protein misfolding.

13 ion protein through a mechanism of templated misfolding.

14 nd neurobiological defects caused by protein misfolding.

15 anism that chaperones may exploit to prevent misfolding.

16 he protein to fold, thereby reducing protein misfolding.

17 ion-dependent proteasomal degradation due to misfolding.

18 be harnessed to reverse deleterious protein misfolding.

19 intermediate that, in turn, facilitates IAPP misfolding.

20 tion into neutral membranes and enhance IAPP misfolding.

21 interactions that may lead to prion protein misfolding.

22 n, possibly due to increased cotranslational misfolding.

23 , moPrP(23-231), under conditions that favor misfolding.

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

25 the microscopic mechanisms governing protein misfolding.

26 MIF is shown to directly inhibit mutant SOD1 misfolding.

27 een physiological interaction and pathogenic misfolding.

28 ation causes defects associated with protein misfolding.

29 stand neurotoxicity induced by prion protein misfolding.

30 human neurodegenerative diseases of protein misfolding.

31 ns and the deleterious consequences of their misfolding.

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

33 ns and the end product of pathologic protein misfolding.

34 ases associated with cell stress and protein misfolding.

35 ty of a given fold to undergo domain-swapped misfolding?

36 exist with islet amyloid polypeptide (IAPP) misfolding, a process central to beta-cell dysfunction a

37 GBA1 mutations commonly result in protein misfolding, abnormal chaperone recognition, and prematur

38 hin the exon1 of huntingtin leads to protein misfolding, aggregation, and cytotoxicity in Huntington'

39 incurable human disease characterized by the misfolding, aggregation, and systemic deposition of amyl

40 ly important because their deterioration and misfolding/aggregation are associated with melanoma tumo

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

42 egenerative diseases are associated with the misfolding and aberrant accumulation of specific protein

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

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

45 urodegenerative diseases associated with the misfolding and accumulation of normal prion protein (PrP

46 the toxicity of mutant SOD1 results from its misfolding and accumulation on the cytoplasmic faces of

47 Heat causes protein misfolding and aggregation and, in eukaryotic cells, tri

48 e of alpha-synuclein (aSyn) and aSyn protein misfolding and aggregation are seen as major factors in

49 ke all membrane proteins, ssMPs are prone to misfolding and aggregation because of the hydrophobicity

50 neurodegeneration associated with cytosolic misfolding and aggregation can be ameliorated by overexp

51 Despite the central role of protein misfolding and aggregation in many diseases, it has prov

52 estosterone), and the polyQ triggers ARpolyQ misfolding and aggregation in spinal cord motoneurons an

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

54 Our data suggest that TrkA misfolding and aggregation induced by some CIPA mutation

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

56 Protein misfolding and aggregation is increasingly being recogni

57 his observation for our understanding of its misfolding and aggregation mechanisms.

58 ) appears to be caused by the misfolding, or misfolding and aggregation of an antibody LC or fragment

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

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

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

62 is accompanied by the proteolytic cleavage, misfolding and aggregation of huntingtin.

63 hereby abnormally folded proteins induce the misfolding and aggregation of like proteins into charact

64 the uptake of pathological tau seeds causing misfolding and aggregation of monomeric tau in recipient

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

66 uIC technique is based on prion seed-induced misfolding and aggregation of recombinant prion protein

67 In particular, misfolding and aggregation of the Josephin domain of ata

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

69 mportance when alpha-synuclein undergoes the misfolding and aggregation reported in PD.

70 cluding Parkinson's disease (PD), is protein misfolding and aggregation that in turn leads to neuroto

71 e of these modifications in inducing protein misfolding and aggregation was determined by inducing ca

72 rtment of different stresses such as protein misfolding and aggregation, hyperosmotic stress, membran

73 eurodegenerative disorders caused by protein misfolding and aggregation, including amyotrophic latera

74 uronal proteostasis, associated with protein misfolding and aggregation, leads to proteinopathies or

75 s a result of evolutionary pressure to avoid misfolding and aggregation, particularly at the high cel

76 operty was selected by evolution to minimize misfolding and aggregation.

77 erapy of pathologies associated with protein misfolding and aggregation.

78 of functional proteins puts them at risk of misfolding and aggregation.

79 es linked to excessive extracellular protein misfolding and aggregation.

80 omeostasis within neurons results in protein misfolding and aggregation.

81 l rearrangements that lead to initial beta2m misfolding and aggregation.

82 ociated mutations in the C1 domain cause its misfolding and aggregation.

83 sical properties of proteins associated with misfolding and aggregation.

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

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

86 revealing volume changes associated with the misfolding and assembly reactions.

87 chanism leading to pathology likely involves misfolding and autophagy, although it has been hypothesi

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

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

90 ociated mutations in MUNC18-1 cause Munc18-1 misfolding and cellular aggregation.

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

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

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

94 in response to age or stress-induced protein misfolding and denaturation.

95 d impaired nerve regenerative response after misfolding and deposition in the peripheral nervous syst

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

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

98 Misfolding and fibril formation of phosphorylated alpha-

99 Protein misfolding and formation of cross-beta structured amyloi

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

101 ytosolic protein, PARK7/DJ-1, causes protein misfolding and is linked to Parkinson disease.

102 BiP functions as a sentinel for protein misfolding and maintains ER homeostasis.

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

104 rface that becomes exposed upon mutated SOD1 misfolding and monomerization.

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

106 rum of brain pathologies elicited by protein misfolding and provides a paradigm for understanding the

107 Protein disaggregases that reverse protein misfolding and restore proteins to native structure, fun

108 ndamental cause of specific disorders is the misfolding and seeded aggregation of certain proteins.

109 The misfolding and self-assembly of amyloid-beta (Abeta) int

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

111 erent multiplicity of the process of protein misfolding and the key role the beta-sheet geometry acqu

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

113 f interest because point mutations result in misfolding and thus cause clinically relevant phenotypes

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

115 tionally destabilized reporters that undergo misfolding and ubiquitylation upon removal of a stabiliz

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

117 Proteome misfolding and/or aggregation, caused by a thermal pertu

118 ed form, which resists tetramer disassembly, misfolding, and aggregation.

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

120 lation between interdomain linker length and misfolding, and propose a simple alchemical model to pre

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

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

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

124 on is important in recovering from transient misfoldings; and that the early formation of long-range

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

126 two prolines, and mutations thereof, on PrP misfolding are not well understood.

127 d stability and increased propensity towards misfolding are the main causes for the loss of SepSecS a

128 l fluctuations are also critical for protein misfolding associated with a range of human diseases.

129 xpression likely protects cells from protein misfolding associated with oxidative stress.

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

131 ed protein exhibits more complex folding and misfolding behaviour than either single mutant, suggesti

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

133 tients with variant CJD (vCJD) using protein misfolding by cyclic amplification, which was apparently

134 les of metal binding and activity in protein misfolding by disease-associated mutants.

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

136 , Tafamidis((R)) and diflunisal, inhibit TTR misfolding by stabilizing native tetrameric TTR; however

137 f a mAb is critical for drug efficacy, while misfolding can impact safety by eliciting unwanted immun

138 ses involved in blood coagulation, and ATIII misfolding can thus lead to thrombosis and other disease

139 Protein misfolding caused by inherited mutations leads to loss o

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

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

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

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

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

145 protein amplification assays-such as protein misfolding cyclic amplification (PMCA)-which are based o

146 riminatory method, which uses serial protein misfolding cyclic amplification (sPMCA).

147 An adapted Protein Misfolding Cyclic Amplification methodology based on the

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

149 orted from the intestinal tract, and protein misfolding cyclic amplification showed that PrP(Sc) in o

150 ced by replicating PrP(Sc) in serial Protein Misfolding Cyclic Amplification using sialidase-treated

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

152 The PMCA (protein misfolding cyclic amplification) assay was able to recap

153 E) converting ability as measured by protein misfolding cyclic amplification, used as a proxy for inf

154 ES) in prion, and potentially other, protein misfolding disease states.

155 Cataract is a protein misfolding disease where the size of the aggregate is di

156 Many protein-misfolding diseases are caused by proteins carrying prio

157 a possible therapeutic strategy for protein misfolding diseases by correcting chaperone binding and

158 m susceptible to misfolding, which underlies misfolding diseases such as alpha1-antitrypsin deficienc

159 used for the investigation of other protein misfolding diseases such as Alzheimer's and Parkinson's

160 n increasingly linked with age-onset protein-misfolding diseases such as Alzheimer's, Parkinson's, an

161 to improve protein function in other protein misfolding diseases.

162 otential to treat a variety of human protein misfolding diseases.

163 al functions, and is central to many protein misfolding diseases.

164 n hallmarks of Alzheimer's and other protein misfolding diseases.

165 ications for protein folding, evolution, and misfolding diseases.

166 exploited here to safely prevent two protein misfolding diseases.

167 r homeostasis can be deteriorated in protein misfolding diseases.

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

169 to development into therapeutics for protein-misfolding diseases.

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

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

172 Amyloidosis is a protein-misfolding disorder characterized by the extracellular d

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

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

175 2D and AD, two of the most prevalent protein misfolding disorders.

176 the Ant1-induced diseases belong to protein misfolding disorders.

177 ection, monitoring and treatment of multiple misfolding disorders.

178 has important implications for human protein misfolding disorders.

179 pathies that are collectively termed protein misfolding disorders.

180 B27 can also "behave badly," misfolding during assembly and leading to endoplasmic re

181 rather than serine 512 provoked transporter misfolding, enhanced association to the ER-chaperone cal

182 domain protein folds exhibit no evidence for misfolding, even when adjacent domains have identical se

183 with both functional binding and deleterious misfolding, evolution may be highly predictable at the l

184 Beyond intradomain misfolding, folding of the full-length protein is furthe

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

186 nucleic acid binding might influence protein misfolding for both disease-related and benign, function

187 scopy revealed marked structural changes and misfolding for the P and PV mutants but few changes for

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

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

190 often leads to capsid misassembly or antigen misfolding, hindering generation of protective immunity.

191 otonergic neurons alone can suppress protein misfolding in C. elegans peripheral tissue.

192 unction and muscle wasting caused by protein misfolding in HD.

193 Moreover, proAVP misfolding in hereditary central diabetes insipidus like

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

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

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

197 CFTR misfolding in the endoplasmic reticulum (ER) or general

198 ased protein synthesis often lead to protein misfolding in the organelle, the accumulation of misfold

199 he role of endogenous MIF in modulating SOD1 misfolding in vivo remains unknown.

200 rPres, which was the first product of PrP(C) misfolding in vivo.

201 to prion diseases) and the study of protein misfolding; in addition, it can potentially be used for

202 perturbations, including heat shock, protein misfolding, integrin engagement, and serum stimulation.

203 By immune-targeting sparsely populated TTR misfolding intermediates (i.e. monomers), we achieved fi

204 by preventing the formation of cross-domain misfolding intermediates by leading the protein along pr

205 We show that selective targeting of misfolding intermediates is an alternative to native sta

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

207 Protein misfolding is a common hypothesis underlying the develop

208 The balance between protein folding and misfolding is a crucial determinant of amyloid assembly.

209 Protein misfolding is a key pathological event in neurodegenerat

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

211 Protein misfolding is common across many neurodegenerative disea

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

213 Protein misfolding is implicated in neurodegenerative diseases s

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

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

216 olding mechanism, we find that the extent of misfolding is not determined by the relative folding rat

217 If protein misfolding is not resolved, cells die.

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

219 ein with multiple biological functions whose misfolding is related to Huntington's disease-modulates

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

221 folding, reflecting local roughening of the misfolding landscape, likely due to increased internal f

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

223 To unveil the protein misfolding mechanism and to understand why some mutation

224 diseases that are caused by the same protein-misfolding mechanism, but they appear to pose different

225 y expected based on the previously described misfolding mechanism, we find that the extent of misfold

226 PV allele to investigate the effects of this misfolding mutation in vivo.

227 nse is emerging as a common theme in protein-misfolding neurodegenerative diseases, with relevant mar

228 in prion diseases and possibly other protein misfolding neurodegenerative diseases.

229 siological conditions, protein oxidation and misfolding occur with very low probability and on long t

230 Once misfolding occurs, the pathogenic isoform polymerizes in

231 cause lethal brain diseases; they arise from misfolding of a cell surface protein, PrP(C) to a form c

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

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

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

235 We also suggest that misfolding of enzymes regulating protein synthesis shoul

236 Huntington's disease is triggered by misfolding of fragments of mutant forms of the huntingti

237 an autosomal dominant disorder triggered by misfolding of huntingtin (HTT) protein with an expanded

238 Observing directly the misfolding of individual dimers into minimal aggregates,

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

240 to predict the propensity for domain-swapped misfolding of multidomain proteins.

241 Misfolding of mutant FUS is implicated in this process,

242 Besides inducing misfolding of native proteins, prions bind nucleic acids

243 al inner membrane and can be derailed by the misfolding of one single protein with or without aggrega

244 The misfolding of proteins and their accumulation in extrace

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

246 plays a significant role in the folding and misfolding of SOD1 in vivo, and they have implications f

247 Misfolding of tau proteins into prions and their propaga

248 The misfolding of the Amyloid-beta (Abeta) peptide into beta

249 condition, results from mutations that cause misfolding of the cartilage oligomeric matrix protein (C

250 nse mutations in the catalytic domain induce misfolding of the enzyme.

251 In particular, misfolding of the mostly alpha-helical cellular prion pr

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

253 Prion disease arises upon misfolding of the normal cellular prion protein, PrP(C),

254 ecular event in prion disease, the templated misfolding of the normal prion protein, PrP(c), to a pat

255 de binding domain (NBD1) of CFTR, results in misfolding of the protein and clearance by cellular qual

256 The resulting misfolding of the protein leads to oligodendrocyte death

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

258 myelin protein 22 (PMP22), the intracellular misfolding of which is known to cause peripheral neuropa

259 Misfolding, oligomerization and accumulation of the huma

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 ate, and manipulations that mitigate protein misfolding or facilitate the clearance of misfolded prot

263 (AL amyloidosis) appears to be caused by the misfolding, or misfolding and aggregation of an antibody

264 ding as a competition between productive and misfolding pathways allows us to fully describe the fold

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

266 ce on both protein stability and on specific misfolding pathways.

267 n of a Tyr-based N-terminal motif or partial misfolding physically associate but do not associate pro

268 have found evidence of mitochondrial protein misfolding post-hypoxia and have found that manipulation

269 pansion accelerates protein aggregation, the misfolding process is frequently instigated by flanking

270 excited states in directing both folding and misfolding processes.

271 nhances the functional surface expression of misfolding-prone alpha1(A322D) subunits, which causes au

272 ts a new strategy to restore proteostasis of misfolding-prone GABAA receptors and, therefore, a poten

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

274 fier of the toxicity of two disease-causing, misfolding-prone proteins, SOD1 and TDP-43.

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

276 onships reflect the implicit threat of toxic misfolding (rather than hormonal function at the recepto

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 ease due to aberrant CA12 glycosylation, and misfolding resulting in loss of AE2 activity.

280 Protein misfolding results in devastating degenerative diseases

281 We found that TrkA mutations induce misfolding, retention in the endoplasmic reticulum (ER),

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

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

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

285 otecting cells from otherwise lethal protein misfolding stress.

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

287 ory, D was found to be 1,000-fold slower for misfolding than for native folding, reflecting local rou

288 rnover, increasing the likelihood of protein misfolding that leads to deposition.

289 implicating that the mutation causes a local misfolding that prevents the precursor from becoming pro

290 rchetype of brain diseases caused by protein misfolding, the most common subtype being sporadic Creut

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

292 odification, leading to irreversible protein misfolding; when cryptic in the protein's microenvironme

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

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

295 tive serpin fold renders them susceptible to misfolding, which underlies misfolding diseases such as

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

297 inetic models previously proposed to explain misfolding, with a specific interpretation of the observ

298 rchetype of brain diseases caused by protein misfolding, with the most common subtype being sporadic

299 activity is regulated indirectly by protein misfolding within the ER.

300 s issue, Bersuker et al. report that protein misfolding without ubiquitylation is sufficient for tran