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 creased generation of proteinase K-resistant prion protein.

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

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

5 s proteotoxicity of disease-associated toxic prion protein.

6 how that tau does not strictly classify as a prion protein.

7 on of an abnormal form (PrP(Sc)) of the host prion protein.

8 models led to an accumulation of aggregated prion protein.

9 e also bioassayed in mice expressing porcine prion protein.

10 ng a p.Glu200Lys (E200K) substitution in the prion protein.

11 D) in neuronal cultures expressing the human prion protein.

12 nal transduction pathways that are linked to prion protein.

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

14 f substrate proteins, including alphaSyn and prion proteins.

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

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

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

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

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

20 A) technique, used for fast amplification of prion protein aggregates, could be adapted for growing a

21 cation efficiency and the thermostability of prion protein aggregates.

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

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

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

25 e generated two strains of recombinant human prion protein amyloid fibrils that show dramatic differe

26 Although this study was limited to synthetic prion protein amyloid fibrils, a similar structural basi

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

28 ional stability between strains of mammalian prion protein amyloid.

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 neration-linked proline substitutions in the prion protein and in presenilin 1 that underlie the deve

32 an atypical synaptic deposition of abnormal prion protein and no kuru plaques.

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

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

35 or native endogenous substrates, such as the prion protein, and correlated with a delay in translocat

36 , oligopeptide repeats are found in multiple prion proteins, and expansion of these repeats increases

37 The prion protein appears to be unusually susceptible to con

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

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

40 ect BSE, even within the presence of scrapie prion protein, are required.

41 ed amplification assay employing recombinant prion protein as a conversion substrate and thioflavin T

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

43 We show that cellular prion protein associates via transmembrane metabotropic

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

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

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

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

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

49 e alpha-helices of the normal, noninfectious prion protein, cellular prion protein (PrP(C)), but evid

50 t that autophagy has an instrumental role in prion protein clearance.

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

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

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

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

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

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

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

58 Structures of the infectious form of prion protein (e.g. PrP(Sc) or PrP-Scrapie) remain poorl

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

60 Toxic prion protein-exposed neuronal cells exhibit dramatic re

61 Despite their high level of cellular prion protein expression, HK cells failed to support inf

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

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

66 es, enriches, and detects disease-associated prion protein from whole blood using stainless steel pow

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

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

69 type profile at polymorphic codon 129 of the prion protein gene (PRNP) from predominantly valine homo

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

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

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

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

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

75 Prion protein gene sequence, molecular, and neuropatholo

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

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

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

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

80 between the strain of the pathogen and host prion protein genotype.

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

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

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

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

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

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

87 wed minimal deposition of disease-associated prion protein in peripheral lymphoreticular tissue.

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

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

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

91 Toxic prion protein-induced NAD(+) depletion results from PARP

92 heterologous ABCA1 reduced the conversion of prion protein into the pathological form upon infection.

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

94 signed stabilization of helix 2 of the mouse prion protein is shown to lead to an increase in global

95 In the complex, the prion protein is unstructured from residue 23 to 116.

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

97 , self-propagating, structural variants of a prion protein isolated from wild strains of the yeast Sa

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

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

100 ted that the interaction between aptamer and prion protein led to variation in electrochemical signal

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

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

103 model to understand neurotoxicity induced by prion protein misfolding.

104 (C) is a key modulator of disease-associated prion protein misfolding.

105 familial, and infectious prion diseases, the prion protein misfolds and aggregates in skeletal muscle

106 IMPORTANCE In prion diseases, the prion protein misfolds and aggregates in the central ner

107 haracterization of two variants of the mouse prion protein (moPrP), the full-length moPrP (23-231) an

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

109 First, the prion protein must form an amyloid nucleus that can recr

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

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

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

113 The effects of variability in prion protein on cross-species prion transmission have b

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

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

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

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

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

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

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

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

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

123 Prion proteins provide a unique mode of biochemical memo

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

125 n of distinct conformations of the misfolded prion protein PrP(Sc).

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

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

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

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

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

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

132 Various studies have identified cellular prion protein (PrP(C)) among the protein cargo in human

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

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

135 the hinged two-domain chain of the cellular prion protein (PrP(C)) exhibits a peculiar charge struct

136 conditions associated with the conversion of prion protein (PrP(C)) from its normal conformation to a

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

138 The cellular prion protein (PrP(C)) has been implicated in several ne

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

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

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

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

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

144 Conversion of prion protein (PrP(C)) into a pathological isoform (PrP(

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

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

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

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

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

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

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

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

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

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

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

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

157 The cellular form of the prion protein (PrP(C)) is found in both full-length and

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

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

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

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

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

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

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

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

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

167 he conformational conversion of the cellular prion protein (PrP(C)) to its misfolded pathogenic form

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

169 studies have shown that anchorless cellular prion protein (PrP(C)) undergoes aberrant post-translati

170 We sought to examine interactions of the prion protein (PrP(C)) with monoaminergic systems due to

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

172 ormal, noninfectious prion protein, cellular prion protein (PrP(C)), but evidence is accumulating tha

173 Abetao exists in several populations, where prion protein (PrP(C))-interacting Abetao is a high mole

174 ysiology by binding to cell surface cellular prion protein (PrP(C)).

175 gates of abnormal conformers of the cellular prion protein (PrP(C)).

176 -chain forms (PrP(Sc)) of misfolded cellular prion protein (PrP(C)).

177 6, 154, and 171 of a sheep's normal cellular prion protein (PrP(C)).

178 our biosensor is a fragment of the cellular prion protein (PrP(C), residues 95-110), a highly expres

179 ic marker for Creutzfeldt-Jakob disease, the prion protein (PrP(CJD)), by means of real-time quaking-

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

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

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

183 nalyzed for the accumulation of pathological prion protein (PrP(Sc)) and prion infectivity by mouse b

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

185 infectious, disease-associated state of the prion protein (PrP(Sc)) changes with colonization of sec

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

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

188 ine's ability to reduce levels of pathogenic prion protein (PrP(Sc)) in mouse cells infected with exp

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

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

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

192 halopathies, consist mainly of the misfolded prion protein (PrP(Sc)).

193 pendent increase in cell-associated abnormal prion protein (PrP(TSE)) when exposed to medium spiked w

194 the presence of disease-associated misfolded prion protein (PrP(TSE)), generally associated with infe

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

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

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

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

199 lated synaptotoxicity can be blocked by anti-prion protein (PrP) antibodies, potentially allowing the

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

201 ronal loss, astrocytic gliosis and extensive prion protein (PrP) deposition in the brain.

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

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

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

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

206 Sheep with prion protein (PrP) gene polymorphisms QQ171 and RQ171 w

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

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

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

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

211 The conversion of the prion protein (PrP) into scrapie PrP (PrP(Sc)) is a cent

212 The self-association of prion protein (PrP) is a critical step in the pathology

213 misfolded and protease-resistant form of the prion protein (PrP) is a key event in prion pathogenesis

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

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

216 al antibodies against defined regions of the prion protein (PrP) led to the clearing of PrP(Sc) in cu

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

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

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

220 o different host species requires compatible prion protein (PrP) primary structures, and even one het

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

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

223 To explore the effects of prion protein (PrP) sequence and structural variations o

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

225 , each of which results in the conversion of prion protein (PrP) to transmissible, pathological forms

226 The prion protein (PrP) undergoes a conformational transform

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

228 The prion protein (PrP), widely recognized to misfold into t

229 the cytotoxicity of oligomers formed by the prion protein (PrP)-derived amyloid peptide PrP(106-126)

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

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

232 prion neurodegenerative diseases, misfolded prion proteins (PrP(Sc)) replicate by redirecting the fo

233 loop region (residues 165-175) in mammalian prion proteins (PrP) influences the conversion from the

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

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

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

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

238 ated with the misfolding of the host-encoded prion protein, PrP(C), into a disease-associated form, P

239 by the structural conversion of the cellular prion protein, PrP(C), into its misfolded oligomeric for

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

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

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

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

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

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

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

247 The disease-specific isoform of the prion protein, PrP(Sc), was observed in nerve fibers of

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

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

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

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

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

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

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

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

256 isease include accumulation of the misfolded prion protein (PrPSc), which is derived from its cellula

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

258 at the beta2-alpha2 loop region of the mouse prion protein (residues 165-175) markedly influences inf

259 The N-terminal region of prion protein (residues 23-90) is required for the forma

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

261 n prion-seeded fibrillization of recombinant prion protein (rPrPSen), is known to be highly specific

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

263 limiting the potential conformations of the prion protein (see Deleault et al. above).

264 bility between the prion strain and the host prion protein sequence.

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

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

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

268 with animal bioassays, but the influence of prion protein structure versus that of host cofactors (e

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

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

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

272 n 1 (Q103) and the prion domain of the yeast prion protein Sup35 (NM), in D. discoideum.

273 idogenic protein, the NM domain of the yeast prion protein Sup35 (Sup35(GPI)).

274 We previously showed that the yeast prion protein Sup35 can access the prion conformation in

275 of infectious amyloid formed from the yeast prion protein Sup35, differences in beta-sheet core size

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

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

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

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

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

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

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

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

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 ve at seeding the conversion of normal human prion protein to an amyloid conformation, perhaps the fi

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

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

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

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

291 ars, therefore, that the native state of the prion protein undergoes substantial fluctuations in enth

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

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

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

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

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

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

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

299 Blocking Abeta binding to cellular prion protein with antibodies prevents the facilitation

300 We detected the BSE prion protein within a large excess of classical, atypic