ライフサイエンスコーパス: prion protein

1 exes (like amyloid-beta, alpha-synuclein and prion-protein).

2 e also bioassayed in mice expressing porcine prion protein.

3 nal transduction pathways that are linked to prion protein.

4 at the N-terminal unstructured domain of the prion protein.

5 creased generation of proteinase K-resistant prion protein.

6 ely of a misfolded protein, now known as the prion protein.

7 cal properties that are not dependent on the prion protein.

8 multichain assemblies of misfolded cellular prion protein.

9 9.7-kDa unglycosylated fragment of the human prion protein.

10 y specimen used to detect protease-resistant prion protein.

11 on dynamics of the Syrian hamster and rabbit prion proteins.

12 s expressing small ruminants or heterologous prion proteins.

13 f substrate proteins, including alphaSyn and prion proteins.

14 haracterized functions for the gene encoding prion protein 2 (Prnd) in CNS blood vessel development a

15 ta arch formed by residues 106 to 145 of the prion protein, a hydrophobic and highly fibrillogenic di

16 n, which instead results only when misfolded prion protein accompanies a specific innate immune respo

17 ationship between disease incubation period, prion protein accumulation, neuroinflammation, and chang

18 te that atypical BSEs present with increased prion protein accumulation, neuroinflammation, and decre

19 Misfolded prion protein aggregates (PrP(Sc)) show remarkable struc

20 emical denaturation perturb the structure of prion protein aggregates differently.

21 In this study, we exposed abnormal prion protein aggregates encompassing the spectrum of hu

22 opathology, regional deposition of misfolded prion protein aggregates in the brain, and size of their

23 cation efficiency and the thermostability of prion protein aggregates.

24 cidates the proposed adjuvant role of RNA in prion protein aggregation and propagation, and thus advo

25 Understanding the fundamentals of prion protein aggregation and the molecular architecture

26 rains and how I138M, I139M, and S143N affect prion protein aggregation kinetics.

27 Therefore, accumulation of misfolded prion protein alone does not define targeting of neurode

28 onalized based on a model for human Y145Stop prion protein amyloid, providing a foundation for unders

29 the structural differences between Y145Stop prion protein amyloids from three species: human, mouse,

30 cs have been observed between the infectious prion protein and alphaS, including its ability to sprea

31 m the characterization of the fungal [Het-s] prion protein and have led to the identification in fung

32 s encoded in the structure of the pathogenic prion protein and propagated by an epigenetic mechanism.

33 Continuous interactions between prion protein and the membrane not only constrain the pr

34 ) shows that an orally administered cellular prion protein antagonist can rescue synaptic and cogniti

35 Self-templating assemblies of the human prion protein are clinically associated with transmissib

36 w that transgenic mice expressing guinea pig prion protein are fully susceptible to vCJD and BSE prio

37 Variants in the PRNP gene that encodes prion protein are strong risk factors for sCJD but, alth

38 isease, regardless of the strain of mouse or prion protein, are expressed predominantly by activated

39 eview, I highlight the discovery of cellular prion protein as a high-affinity receptor for Abeta olig

40 We show that cellular prion protein associates via transmembrane metabotropic

41 HDX studies on the human and Syrian hamster prion proteins at a higher pH, various segments of moPrP

42 The prion protein both removes Abeta from the brain and tran

43 ased on its activation by Abeta via cellular prion protein but also due to its known interaction with

44 Therefore, host factors independent of the prion protein can affect prion diversity.

45 ls, including overexpression of the cellular prion protein CD230/PrP(C) and the immunosuppressive cel

46 g conformational variant of the host encoded prion protein cellular (PrPC).

47 s several subtypes as defined by genetic and prion protein characteristics, which are associated with

48 he lysosome function and regulates misfolded prion protein clearance.

49 d-PriSCA_MRI + Gen-includes knowledge of the prion protein codon 129 genotype, a major determinant of

50 the kinetics of prion replication occur in a prion protein codon 129 genotype-dependent manner, refle

51 d, it is largely accepted that variations in prion protein conformation drive the molecular changes l

52 Most yeast prion proteins contain glutamine/asparagine (Q/N)-rich p

53 going debate regarding structural aspects of prion protein conversion and molecular architecture of m

54 ence of membrane-associated, disease-causing prion protein (Ctm)PrP, increased ALIX and ALG-2 levels

55 tides with an elevated level of their normal prion protein dendritic receptor and of phospho-tau spec

56 gnificantly augmented proteinase K-resistant prion protein deposition and accelerated prion disease p

57 d by the host genotype, spleen material with prion protein deposition from a PRNP 129 methionine/vali

58 le spongiform encephalopathy vacuolation and prion protein deposition) were analysed and biochemical

59 loid angiopathy and did not co-localize with prion protein deposition.

60 The prion protein-encoding gene (PRNP) is one of the major d

61 Toxic prion protein-exposed neuronal cells exhibit dramatic re

62 The prion protein family member Doppel, which possesses a th

63 In contrast, another prion protein family member, Shadoo (Sho), a natively di

64 we have investigated the effect of Cu(II) on prion protein folding and its coordination geometries wh

65 rapid substrate than either bovine or human prion protein for propagating BSE and vCJD prions.

66 her mammalian species, the normal "cellular" prion protein ([Formula: see text]) is transformed into

67 Our findings extend the knowledge of current prion proteins from cellular organisms to non-cellular l

68 hat TNTs facilitate the exchange of viral or prion proteins from infected to naive cells, it is not c

69 u), bank vole (BV), and Syrian hamster (SHa) prion protein, from disordered monomers to beta-sheet-ri

70 rion diseases require host expression of the prion protein gene (PRNP) and a range of other cellular

71 We examined the prion protein gene (PRNP) in North American elk (Cervus

72 ) that expresses the elk (Cervus canadensis) prion protein gene (PRNP).

73 different host species that express the same prion protein gene (Prnp).

74 genetic diagnosis is a P102L mutation of the prion protein gene (PRNP).

75 ve disorder associated with mutations in the prion protein gene and accumulation of misfolded PrP wit

76 pairings of the genotype at codon 129 of the prion protein gene and conformational properties of the

77 Single nucleotide polymorphisms within the prion protein gene have been linked to differential susc

78 Prion protein gene sequence, molecular, and neuropatholo

79 , provides a unified framework for analyzing prion protein gene variability and spatial structure.

80 y in two hosts species that express the same prion protein gene.

81 by a pathogenic mutation at codon 102 in the prion protein gene.

82 There are 2 allelic variants in the elk prion protein gene: L132 (leucine) and M132 (methionine)

83 opensity is influenced neither by sex nor by prion protein genotype at codon 96; and (iii) the source

84 upon infection of the same host species and prion protein genotype, our findings indicate that certa

85 d transgenic (Tg) mice expressing guinea pig prion protein (GPPrP).

86 tabotropic glutamate receptor 5 and cellular prion protein has a central role in Alzheimer's disease

87 e strains in mice expressing human or bovine prion protein has been difficult because of prolonged in

88 accumulations of abnormally folded cellular prion protein in affected tissues.

89 e amounts of the disease-specific pathologic prion protein in cerebrospinal fluid (CSF) or olfactory

90 it properties similar to those of infectious prion protein in experimental systems: discrete and self

91 in FFI and novel characteristics of natural prion protein in FFI, altered PrPres and Scrapie PrP (ab

92 -CSF) for highly efficient detection of TSEs prion protein in goat cerebrospinal fluid.

93 t distinguishes cells carrying a model yeast prion protein in its nonprion and prion forms.

94 rodegenerative disorders caused by misfolded prion protein in the brain.

95 ncluding two not followed clinically) showed prion protein in the substantia gelatinosa, spinothalami

96 port has described the detection of abnormal prion protein in the urine of patients with variant CJD

97 CJD, for the detection of disease-associated prion protein in urine samples from patients with sCJD.

98 promoting lysosomal degradation of misfolded prion proteins in cancer cells.

99 In vivo, toxic prion protein-induced degeneration of hippocampal neuron

100 Cellular prion protein interacts with copper, Cu(II), through oct

101 disorders caused by misfolding of the normal prion protein into an infectious cellular pathogen.

102 Our results suggest that the guinea pig prion protein is a better, more rapid substrate than eit

103 Scrapie prion protein is a misfolded and aggregated form of PrP(

104 As expected, the degradation rate of the prion protein is significantly decreased upon aggregatio

105 es, enriches, and detects disease-associated prion protein isoforms.

106 binds various conformations of the cellular prion protein, leading us to question the role of fH in

107 bly, induced by structural misfolding of the prion proteins, leads to a number of neurodegenerative d

108 ansduction pathways that have been linked to prion protein may provide a mechanism for intervention.

109 ting molecular interactions that may lead to prion protein misfolding.

110 model to understand neurotoxicity induced by prion protein misfolding.

111 nd tertiary structural segments of the mouse prion protein (moPrP) were monitored independently, afte

112 tion of the N state of the full-length mouse prion protein, moPrP(23-231), under conditions that favo

113 The prion protein N-terminal cleavage fragment, N1, has demo

114 ce expressing human prion protein on a mouse prion protein null background, the temporal distribution

115 s prion aggregate, PrP(Sc), and the cellular prion protein of the host, PrP(C) A puzzling feature of

116 barriers in transgenic mice expressing human prion protein on a mouse prion protein null background,

117 Recent studies revealed that cellular prion protein on neurons bind Alzheimer's amyloid-beta o

118 but was unrelated to the expression of host prion protein or its pathologic amyloid form.

119 an be rescued by blockade of either cellular prion protein or metabotropic glutamate receptor 5.

120 of misfolded, self-replicating states of the prion protein or PrP(C) PrP(C) is posttranslationally mo

121 ing states of a sialoglycoprotein called the prion protein or PrP(C) The current work tests a new hyp

122 ggregated form of a sialoglycoprotein called prion protein or PrP(C).

123 ovide evidence that, in addition to cellular prion protein, other region- and species-specific molecu

124 ondrial dysfunction, possibly exacerbated by prion protein overexpression, occurs at late stages duri

125 tigates the early-stage aggregation of three prion protein peptides, corresponding to residues 120-14

126 is effort, we previously reported that mouse prion protein-promoter-driven, ubiquitous expression of

127 lational modifications impact the aggregated prion protein properties and disease phenotype.

128 Prion proteins provide a unique mode of biochemical memo

129 d in distinct conformations of the misfolded prion protein PrP(Sc) This concept is largely based on i

130 ee distinct beta-sheet-rich oligomers of the prion protein PrP, a protein characterized by a variety

131 case of the infectious form of the mammalian prion protein PrP.

132 lenges and determine D for misfolding of the prion protein PrP.

133 ic peptides, namely, the 106-126 fragment of prion protein (PrP(106-126)) and the human islet amyloid

134 d residue at position 163 of canine cellular prion protein (PrP(C) ) is a major determinant of the ex

135 with amyloid beta (Abeta) and with cellular prion protein (PrP(C) ) were also assessed with IHC and

136 ble substrate for binding Abeta and cellular prion protein (PrP(C) ), the protein that is thought to

137 by TUDCA treatment, TUDCA-mediated cellular prion protein (PrP(C)) activation was assessed.

138 naptic receptor complex composed of cellular prion protein (PrP(C)) and metabotropic glutamate recept

139 The cellular prion protein (PrP(C)) comprises two domains: a globular

140 idylinositol (GPI) membrane anchoring of the prion protein (PrP(C)) directs it to specific regions of

141 It has been proposed that the cellular prion protein (PrP(C)) functions as a cell-surface recep

142 The prion protein (PrP(C)) has been suggested to operate as

143 Over the past decade, the cellular prion protein (PrP(C)) has emerged as an important media

144 d interactions, given the location of normal prion protein (PrP(C)) in lipid rafts and lipid cofactor

145 el, we show increased expression of cellular prion protein (PrP(C)) in schwannoma cells and tissues.

146 lphosphatidylinositol (GPI) anchoring of the prion protein (PrP(C)) influences PrP(C) misfolding into

147 folding of the mostly alpha-helical cellular prion protein (PrP(C)) into a beta-sheet-rich disease-ca

148 ers caused by the misfolding of the cellular prion protein (PrP(C)) into cytotoxic fibrils (PrP(Sc)).

149 cur following the conversion of the cellular prion protein (PrP(C)) into disease-related isoforms (Pr

150 rlying conformational conversion of cellular prion protein (PrP(C)) into its infectious counterpart (

151 th the misfolding and accumulation of normal prion protein (PrP(C)) into its pathogenic scrapie form

152 capable of transforming the normal cellular prion protein (PrP(C)) into new infectious PrP(Sc) Inter

153 Structural conversion of cellular prion protein (PrP(C)) into scrapie PrP (PrP(Sc)) and su

154 block conversion of the cellular form of the prion protein (PrP(C)) into the infectious isoform (PrP(

155 The autocatalytic conversion of the cellular prion protein (PrP(C)) into the pathologic isoform PrP(S

156 animals caused by misfolding of the cellular prion protein (PrP(C)) into the pathological isoform PrP

157 nfected individuals by converting the normal prion protein (PrP(C)) into the pathological isoform.

158 We reported previously that the cellular prion protein (PrP(c)) is a component of desmosomes and

159 The cellular prion protein (PrP(C)) is a glycoprotein that is process

160 The cellular form of the prion protein (PrP(C)) is a highly conserved glycoprotei

161 The cellular prion protein (PrP(C)) is a key neuronal receptor for be

162 Cellular prion protein (PrP(C)) is a mammalian glycoprotein which

163 Cellular prion protein (PrP(C)) is a widely expressed glycosylpho

164 The cellular prion protein (PrP(C)) is a zinc-binding protein that co

165 nonpathogenic cellular isoform of the human prion protein (PrP(c)) is an adhesion molecule constitut

166 The cellular prion protein (PrP(C)) is associated with metastasis, tu

167 Although the cellular prion protein (PrP(C)) is concentrated at synapses, the

168 The prion protein (PrP(C)) is highly expressed in the nervou

169 Because the cellular prion protein (PrP(C)) is required for propagation of th

170 The initial report that cellular prion protein (PrP(C)) mediates toxicity of amyloid-beta

171 ions of cervid species that express cellular prion protein (PrP(C)) molecules varying in amino acid c

172 tive deletion of the Abetao-binding cellular prion protein (PrP(C)) prevents development of memory de

173 uted, the physiological role of the cellular prion protein (PrP(C)) remains enigmatic.

174 The normal cellular prion protein (PrP(C)) resides in detergent-resistant ou

175 gomeric amyloid-beta-Abetao-binding cellular prion protein (PrP(C)) signaling pathway in a familial f

176 rP-scrapie (PrP(Sc)), a misfolded isoform of prion protein (PrP(C)) that accumulates in the neuroreti

177 Sc)) replicate by inducing a normal cellular prion protein (PrP(C)) to adopt the prion conformation.

178 The susceptibility of the cellular prion protein (PrP(C)) to convert to an alternative misf

179 ity of the host-encoded cellular form of the prion protein (PrP(C)) to selectively propagate optimize

180 Here, we investigated whether the prion protein (PrP(C)), a neuronal protein known to modu

181 , including aberrant neuronal activity, tau, prion protein (PrP(C)), and EphB2 itself.

182 f 15 reported Abeta receptors, only cellular prion protein (PrP(C)), Nogo receptor 1 (NgR1), and leuk

183 6, 154, and 171 of a sheep's normal cellular prion protein (PrP(C)).

184 PrP(Sc), a misfolded version of the cellular prion protein (PrP(C)).

185 ) relies on immunodetection of misfolded CWD prion protein (PrP(CWD)) by western blotting, ELISA, or

186 The presence of abnormal, disease-related prion protein (PrP(D)) has recently been demonstrated by

187 Protease-resistant prion protein (PrP(res)) accumulation in lymphoreticular

188 P allotype composition in protease-resistant prion protein (PrP(res)) from brain of heterozygous ARR/

189 To detect disease-associated prion protein (PrP(Sc) ) in the vagus nerve in different

190 ecropsy were examined for disease-associated prion protein (PrP(Sc)) by Western blotting (WB), antige

191 ostic nerve biopsies and looked for abnormal prion protein (PrP(Sc)) by western blotting and real-tim

192 ationship between the transport of misfolded prion protein (PrP(Sc)) from the brain to the retina, th

193 Misfolded and aggregated forms of the prion protein (PrP(Sc)) have been associated with many p

194 Prions are composed of the misfolded prion protein (PrP(Sc)) organized in a variety of aggreg

195 Disease-associated prion protein (PrP(Sc)) was detected in brain and lympho

196 ive disorders caused by an abnormally folded prion protein (PrP(Sc)).

197 biochemical properties of disease-associated prion protein (PrP(Sc)).

198 are composed of pathogenic conformers of the prion protein (PrP(TSE)).

199 tion in humans and animals depends on single prion protein (PrP) amino acid substitutions in the host

200 ere the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syria

201 Most pure recombinant prion protein (PrP) amyloids generated in vitro are not

202 o address the question of cross-talk between prion protein (PrP) and Alzheimer's disease (AD), we gen

203 Mutations in the gene encoding the prion protein (PrP) are responsible for approximately 10

204 n which a single gene gives rise to a single prion protein (PrP) capable of converting into the sole

205 Amino acid sequence variants of the prion protein (PrP) determine transmissibility in the ho

206 The prion protein (PrP) evolved from the subbranch of ZIP me

207 Lowering of prion protein (PrP) expression in the brain is a genetic

208 be induced by in vitro-produced recombinant prion protein (PrP) fibrils with structures that are fun

209 ral features that confer transmissibility to prion protein (PrP) fibrils, we have analyzed synthetic

210 somal dominant coding mutations in the human prion protein (PrP) gene (PRNP) and account for about 15

211 SE caused by a range of mutations within the prion protein (PrP) gene.

212 The prion protein (PrP) has been implicated both in prion di

213 of a misfolded isoform of the host cellular prion protein (PrP) in the brain.

214 ymerization of tau, alpha-synuclein, and the prion protein (PrP) induced by aggregates in biospecimen

215 The conversion of normal prion protein (PrP) into pathogenic PrP conformers is ce

216 Prion protein (PrP) is found in all mammals, mostly as a

217 Prion protein (PrP) is found in all mammals, usually att

218 By engineering knockin mice expressing prion protein (PrP) lacking 2 N-linked glycans (Prnp180Q

219 Reduction of native prion protein (PrP) levels in the brain is an attractive

220 D) is a neurodegenerative disorder caused by prion protein (PrP) misfolding, clinically recognized by

221 Familial prion protein (PrP) mutants undergo conversion from solu

222 ed effects of prion seeding and mutations of prion protein (PrP) on the structure and transmission pr

223 Misfolded prion protein (PrP) seeds were observed widespread throu

224 The prion protein (PrP) seems to exert both neuroprotective

225 sleep through a pharmacologically tractable Prion Protein (PrP) signaling cascade.

226 Although the amino acid residues of the prion protein (PrP) that prevent or permit human CWD inf

227 caused by conformational corruption of host prion protein (PrP) to its infective counterpart, contag

228 first transgenic mouse model expressing dog prion protein (PrP) was generated and challenged intrace

229 Prions derived from the prion protein (PrP) were first characterized as infectio

230 tichain assemblies of misfolded host-encoded prion protein (PrP), act as lethal infectious agents, Pr

231 caused by misfolding and aggregation of the prion protein (PrP), and there are currently no therapeu

232 mational change of the host-encoded cellular prion protein (PrP), leading to the formation of beta-sh

233 composed of assemblies of misfolded cellular prion protein (PrP).

234 and multimeric forms of the normal cellular prion protein (PrP).

235 We have used misfolded prion protein (PrP*) as a model to investigate how mamma

236 The wild type prion protein (PrP-WT), having an intact flexible part,

237 Misofolding of mammalian prion proteins (PrP) is believed to be the cause of a gr

238 rospinal fluid analysis) and molecular data (prion protein [PrP] gene sequencing, PrPSc type).

239 that the amino-terminal domain of the normal prion protein, PrP(c), hinders seeded conversion of bovi

240 y a structural rearrangement of the cellular prion protein, PrP(C), into a disease-associated conform

241 rises upon misfolding of the normal cellular prion protein, PrP(C), into the disease-associated isofo

242 The cellular prion protein, PrP(C), is attached by a glycosylphosphat

243 ease, the templated misfolding of the normal prion protein, PrP(c), to a pathogenic, amyloid isoform,

244 g glycophosphatidylinositol (GPI)-anchorless prion protein, PrP(C), together with hydrogen-deuterium

245 ated with infectious, misfolded forms of the prion protein, PrP(res) We show that only GPI-anchored P

246 ), to a pathogenic, amyloid isoform, scrapie prion protein, PrP(Sc) We examined the role of the PrP(c

247 The structure of the infectious form of prion protein, PrP(Sc), remains unclear.

248 ses (valine homozygosity at codon 129 of the prion protein, PrP, gene harboring disease-related PrP,

249 ek BSE-Scrapie Ag Kit to detect the abnormal prion protein, PrP.

250 accumulation of pathological isoforms of the prion protein, PrP.

251 Recombinant C-terminally truncated prion protein PrP23-144 (which corresponds to the Y145St

252 disorders pathogenically linked to cellular prion protein (PrPC) misfolding into abnormal conformers

253 Levels of normal cellular prion protein (PrPc), a receptor for amyloid peptides, a

254 ed with neurodegenerative diseases including prion protein (PrPC), tau, and alpha-synuclein.

255 PrPSc) converted from a normal host cellular prion protein (PrPC).

256 any of the cytotoxic effects of these mutant prion proteins (PrPDeltaHD and PrPDeltaCR) when coexpres

257 rvable effect on gliosis, protease-resistant prion protein (PrPres) formation, disease tempo, patholo

258 aracterized by the accumulation of misfolded prion protein (PrPSc) converted from a normal host cellu

259 rders characterized by deposition of scrapie prion protein (PrPSc) in the CNS.

260 ing prion infection, host protease-sensitive prion protein (PrPsen or PrPC) is converted into an abno

261 en bound to the non-OR region of recombinant prion proteins (recPrP) from mammalian species considere

262 how they or other PQC factors interact with prion proteins remains unclear.

263 the genetic and physical interaction of the prion protein Rnq1 with Sup35 as a predominant mechanism

264 ce the aggregation of the murine recombinant prion protein (rPrP).

265 inant derivative of PrP(C) (soluble cellular prion protein, S-PrP) that corresponds closely in sequen

266 vation in the detection of abnormally folded prion protein scrapie (PrP(Sc)) in human brain and cereb

267 ent is unique in biology and is comprised of prion protein scrapie (PrPSc), a self-templating conform

268 PrP(C), the cellular isoform of the prion protein, serves to transduce the neurotoxic effect

269 hat the strictly conserved Y169 in mammalian prion proteins stabilizes the 310-helical turn in the be

270 for fitness costs of the 132L allele or new prion protein strains to arise suggest that it is pruden

271 able brain disorder caused by alterations in prion protein structure.

272 ed misfolding and aggregation of recombinant prion protein substrate, accelerated by alternating cycl

273 the reactivities with different recombinant prion protein substrates and/or immunoblot band profiles

274 n N-terminal hepta-peptide sequence of yeast prion protein Sup35 with the sequence GNNQQNY is widely

275 For the Saccharomyces cerevisiae prion protein Sup35, these different activities are enco

276 n intrinsically disordered region, the yeast prion protein Sup35.

277 The yeast prion protein Sup35NM is a self-propagating amyloid.

278 ed from the yeast (Saccharomyces cerevisiae) prion protein Sup35NM.

279 rrier strength and specificity for the yeast prion protein Sup35p from three closely related species

280 d transgenic mice overexpressing the hamster prion protein (Tg7 mice) suffer from mitochondrial respi

281 y ill transgenic mice overexpressing hamster prion protein (Tg7) infected with the hamster prion stra

282 unconventional agents composed of misfolded prion protein that cause fatal neurodegenerative disease

283 ns are pathological isoforms of the cellular prion protein that is responsible for transmissible spon

284 structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is hig

285 with the accumulation of infectious abnormal prion protein through a mechanism of templated misfoldin

286 ble of seeding the conversion of full-length prion protein to the infectious form has important impli

287 Coupling of cellular prion protein to these intracellular proteins is modifie

288 We used a highly toxic misfolded prion protein (TPrP) model to understand neurotoxicity i

289 Moreover, since the most thermostable prion protein types were those associated with the most

290 rtificial glycans to uniformly (15)N labeled prion protein using a buffer system that evolves over a

291 nt with Creutzfeldt-Jakob disease expressing prion protein valine 129.

292 tro in seeded fibrillization of the Y145Stop prion protein variant.

293 The N state of the prion protein was observed to be at equilibrium with at

294 s, groups of Tg12 mice that express M132 elk prion protein were inoculated intracranially with brain

295 l dynamics of the full-length (23-231) mouse prion protein were studied under native conditions, usin

296 neurological disease caused by an infectious prion protein, which affects economically and ecological

297 he accumulation of the misfolded form of the prion protein, which is followed by the induction of end

298 ce similarity with the central domain of the prion protein, which is key to the formation of mammalia

299 e proteins show sequence similarity to yeast prion proteins, which can interconvert between an intrin

300 , the most common polymorphic version of the prion protein within this animal species.