ライフサイエンスコーパス: Abeta(1 42)

1 urotoxic and myelinotoxic in the presence of Abeta1-42 .

2 urons compared with the full-length isoform (Abeta(1-42)).

3 ant of the Alzheimer's amyloid-beta peptide (Abeta(1-42)).

4 e new molecules can delay the aggregation of Abeta1-42.

5 pro-domain is toxic only in the presence of Abeta1-42.

6 res a neurotoxic activity in the presence of Abeta1-42.

7 brain changes and abnormal levels of plasma Abeta1-42.

8 wed that SUCLG2 was involved in clearance of Abeta1-42.

9 ase and produced varying ratios of Abeta1-40:Abeta1-42.

10 nts and occurs at either Lys-16 or Lys-28 of Abeta1-42.

11 c approaches against neurotoxic CEL-glycated Abeta1-42.

12 ted with cerebrospinal fluid (CSF) levels of Abeta1-42.

13 for identical peptides, such as Abeta1-40 or Abeta1-42.

14 ryptophan within SST14 and the N-terminus of Abeta1-42.

15 and native or oxidized amyloid beta-peptide (Abeta1-42).

16 the cells at low nanomolar concentration of Abeta(1-42).

17 ngly reduced brain efflux of injected [125I] Abeta(1-42).

18 were significantly greater than those of LMW-Abeta(1-42).

19 t protection against neuron death induced by Abeta(1-42).

20 ssion upon exposure of neurons to oligomeric Abeta(1-42).

21 th Bim to induce neuron death in response to Abeta(1-42).

22 eta protein (Abeta), particularly neurotoxic Abeta(1-42).

23 isease with toxicities mimicked by synthetic Abeta(1-42).

24 a4beta2 nAChR-transfected cells treated with Abeta(1-42).

25 g the presence of a ternary complex TTR/IDIF/Abeta(1-42).

26 l forming properties between Abeta(1-40) and Abeta(1-42).

27 and fibrillar forms of both Abeta(1-40) and Abeta(1-42).

28 ted with the older age (0.008) and lower CSF Abeta1-42 (0.005) at baseline.

29 rimers and Abeta*56 (r > 0.63), but not with Abeta1-42 (-0.10 < r < -0.01).

30 A TTR/Abeta(1-42) (1:1) complex with a dissociation constant o

31 CSF Abeta(1-42/1-40) and plasma NFL values changed in indivi

32 beta peptides 1-42 and 1-40 and their ratio (Abeta(1-42/1-40)), total tau protein, and neurofilament

33 ns per week) decreased total brain-insoluble Abeta1-42 (-33%), assessed by ELISA, and the number and

34 molecular architecture of a fibril formed by Abeta(1-42), a particularly pathogenic variant of Abeta

35 wed stronger relationships with tau than did Abeta1-42, a surrogate for Abeta fibril deposition.

36 ntly prevented fibrillation and formation of Abeta(1-42), Abeta(1-40), and alpha-synuclein aggregates

37 When combined in a ratio of 1:9 Abeta(1-42)/Abeta(1-40) to mimic physiologically relevan

38 creased extracellular amyloid deposition and Abeta1-42/Abeta1-40 ratio, prevented the development of

39 noncarriers, 13.1 [3.2] pg/mL; P < .001) and Abeta1-42:Abeta1-40 ratios (mean [SD]: carriers, 0.32 [0

40 included plasma Abeta1-42 concentrations and Abeta1-42:Abeta1-40 ratios, memory encoding-dependent ac

41 myloid imaging and cerebrospinal fluid (CSF) Abeta1-42 (Abeta42) is an early indicator of preclinical

42 In particular, soluble Abeta(1-42) acutely inhibits LTP and chronically causes

43 Here we quantify binding to PrP of Abeta(1-42) after different durations of aggregation.

44 t age 20 years (95% CI, 14-24 years) for CSF Abeta1-42, age 16 years (95% CI, 11-24 years) for the me

45 beta-Sheet-rich Abeta(1-42) aggregates entered the cells at low nanomola

46 concentrations and time scales that allowed Abeta(1-42) aggregates to form.

47 Here we show that, when Abeta(1-42) aggregates, including fibrils, are bound to

48 que to characterize the in vitro kinetics of Abeta(1-42) aggregation by measuring the size distributi

49 We also show a reduced level of Abeta(1-42) aggregation with A2T Abeta peptides, an obse

50 moderate to high inhibition of AChE-induced Abeta1-42 aggregation and noticeable in vitro antioxidan

51 ture structure-based design of inhibitors of Abeta1-42 aggregation.

52 ctrometry (MS) to monitor the time-course of Abeta1-42 aggregation.

53 er, the HS-like molecule heparin facilitated Abeta1-42-aggregation in an in vitro Thioflavin T assay.

54 of A2V Abeta1-6 (Abeta6) hexapeptide and WT Abeta1-42 (Alphabeta42) is also found neuroprotective.

55 ly less effective, particularly in degrading Abeta(1-42), although the targeted peptide bonds were id

56 Mitophagy diminishes insoluble Abeta(1-42) and Abeta(1-40) and prevents cognitive impai

57 The rate constants differ markedly between Abeta(1-42) and Abeta(1-40), with Abeta(1-42) showing a

58 Here we compared the impacts of Abeta(1-42) and monastrol, a small-molecule Eg5 inhibito

59 red using Elecsys CSF immunoassays, and tTau/Abeta(1-42) and pTau/Abeta(1-42) ratios calculated.

60 assessed using pre-established cut-offs for Abeta(1-42) and ratios; tTau and pTau cut-offs were dete

61 mbrane potential, an effect recapitulated by Abeta(1-42) and reversed by nimodipine.

62 ession, blocked the neurocytotoxic effect of Abeta(1-42) and significantly increased cell viability.

63 f TREM2 serves as a compensatory response to Abeta(1-42) and subsequently protects against AD progres

64 aggregate formation of fluorescently labeled Abeta(1-42) and tracked its internalization by human neu

65 Elecsys pTau/Abeta(1-42) and tTau/Abeta(1-42) are robust biomarkers f

66 Cerebrospinal fluid amyloid-beta 1-42 (Abeta1-42) and phosphorylated Tau at position 181 (pTau1

67 nteraction between the amyloid-beta peptide (Abeta1-42) and the pro-domains of both DNT1 and BDNF.

68 variable, given that the association between Abeta1-42 and Abeta1-40 and cognitive impairment was onl

69 alogue) showed lower binding affinity toward Abeta1-42 and Abeta1-40 fibrils than its neutral analogu

70 Full-length Abeta1-42 and Abeta1-40, N-truncated pyroglutamate Abeta

71 e found significant interactions between CSF Abeta1-42 and CSF clusterin, as well as CSF Abeta1-42 an

72 Abeta1-42 and CSF clusterin, as well as CSF Abeta1-42 and CSF p-tau181p, on the entorhinal cortex at

73 hippocampal neurons treated with oligomeric Abeta1-42 and cultured from 5XFAD mice.

74 Soluble Abeta1-42 and fibrillar Abeta measured by [(3)H] Pittsbu

75 Abeta1-42 and hAmylin also induce cell death during expo

76 with PD by their motor phenotypes, lower CSF Abeta1-42 and P-tau181 concentrations were associated wi

77 ate regression analysis, we found that lower Abeta1-42 and P-tau181 levels were associated with PD di

78 sis of genome-wide association study data on Abeta1-42 and pTau181 in AD dementia patients followed b

79 se increases phagocytic uptake of oligomeric Abeta1-42 and stimulates lysosomal Abeta1-42 degradation

80 two hallmark molecular pathologies: amyloid abeta1-42 and Tau neurofibrillary tangles.

81 y, diffuse deposits display higher levels of Abeta1-42 and that Abeta plaque maturation over time is

82 iotensin-converting enzyme (ACE) can degrade Abeta(1-42), and ACE overexpression in myelomonocytic ce

83 alpha-synuclein, but not beta-amyloid 1-42 (Abeta1-42), and lower concentration of CSF biomarkers, a

84 een cerebrospinal fluid (CSF) clusterin, CSF Abeta1-42, and CSF p-tau at threonine 181 (p-tau181p) on

85 high neurofilament light chain protein, low Abeta1-42, and high heart fatty acid-binding protein at

86 high neurofilament light chain protein, low Abeta1-42, and high heart fatty acid-binding protein wer

87 ecause the steady-state levels of Abeta1-40, Abeta1-42, and soluble AbetaPP beta were the same in 2-

88 This study investigates the impact of acute Abeta1-42 application on GABAergic synaptic transmission

89 in patients with sporadic PD, low levels of Abeta(1-42) are associated with a higher risk of develop

90 Elecsys pTau/Abeta(1-42) and tTau/Abeta(1-42) are robust biomarkers for predicting risk of

91 which was estimated with cerebrospinal fluid Abeta1-42 as the reference standard.

92 s, a positive association between amylin and Abeta1-42 as well as Abeta1-40 is found only in patients

93 We demonstrate that for Abeta(1-40), and Abeta(1-42), as little as 0.01mol equivalent of Zn(2+) (

94 Our data indicated that Abeta(1-42) assemblies in oligomeric preparations form v

95 ly synthesizing defined CEL modifications on Abeta1-42 at Lys-16 (Abeta-CEL16), Lys-28 (Abeta-CEL28),

96 th by allowing the conformational changes of Abeta1-42 at subregional and even amino-acid-residue lev

97 e monitoring of the solvent accessibility of Abeta1-42 at various stages of oligomerization, and prov

98 of 153 MCI patients with cerebrospinal fluid Abeta1-42 biomarker data but no amyloid PET scans.

99 h Abeta peptides, we found that high dose of Abeta1-42 but not Abeta1-40 significantly decreased Ptc1

100 agocytosis and degradation amyloid beta1-42 (Abeta1-42), but are improved by omega-3 fatty acids (ome

101 Notably, Abeta1-42, but not Abeta1-40, formed in the presence of

102 Here we describe footprinting of Abeta1-42 by hydroxyl radical-based fast photochemical o

103 Our results indicate that USPIO-PEG-Abeta1-42 can be used for amyloid plaque detection in vi

104 In contrast, Abeta(1-42) caused a significant elevation in cytosolic

105 nd for a closely related control peptide for Abeta1-42 cellular studies of disease pathology, offerin

106 le model of ring-like assemblies of S-shaped Abeta1-42 chains and study the stability and structural

107 In this study, we found that plasma Abeta(1-42) concentration increases with age, while the

108 Outcome measures included plasma Abeta1-42 concentrations and Abeta1-42:Abeta1-40 ratios,

109 Abeta plaque accumulation, reduction of CSF Abeta1-42 concentrations, and hippocampal atrophy (struc

110 ospinal fluid and has a similar abundance to Abeta(1-42), constituting one-fifth of the plaque load.

111 Our findings demonstrate that only Abeta(1-42) contains unique structural features that fac

112 id MVs were associated with Tau but not with Abeta1-42 CSF levels.

113 us PET cutoff values and the established CSF Abeta1-42 cutoff levels.

114 of sub-pathological dose of Abeta (160 pmol Abeta1-42/day i.c.v) for 14 days.

115 ligomeric Abeta1-42 and stimulates lysosomal Abeta1-42 degradation in cultured microglia and in vivo.

116 rmation, whereas CEL glycations at Lys-16 of Abeta1-42 delayed fibril formation.

117 Finally, in an in vivo Drosophila model of Abeta(1-42) dependent toxicity, D-520 exhibited efficacy

118 HMW-Abeta(1-42) disturbed membrane integrity by inducing ROS

119 and fibrillar states of amyloid-beta(1-42) (Abeta(1-42)) during Alzheimer's disease.

120 sugar-based peptidomimetics to inhibit both Abeta1-42 early oligomerization and fibrillization.

121 Molecular recognition studies with IAPP and Abeta1-42 employing saturation transfer difference (STD)

122 mechanisms of neuronal dysfunction from HMW-Abeta(1-42) exposure by measuring membrane integrity, re

123 lcium concentration ([Ca(2+)](i)), following Abeta(1-42) exposure, caused the activation of calpain t

124 ted in neurons upon toxic beta-amyloid 1-42 (Abeta(1-42)) exposure both in vitro and in vivo.

125 aggregation modulators TAE-1 and TAE-2 with Abeta(1-42) fibrils performed using Autodock Vina sugges

126 For Abeta(1-42) fibrils, we observed similar NMR lineshapes

127 Treatment with either Abeta1-42 monomer or Abeta1-42 fibrils did not induce senescence in this assa

128 tyryl-BTDs showed higher binding affinity to Abeta1-42 fibrils than to Abeta1-40 fibrils.

129 treatment, 5 uM Abeta1-42 monomers, and 5 uM Abeta1-42 fibrils, respectively.

130 suggesting a potential mechanism for the CSF Abeta1-42 findings.

131 new insights on site-specific aggregation of Abeta1-42 for a sample state beyond the capabilities of

132 ing mouse alpha4beta2-nAChRs were exposed to Abeta1-42 for intervals from 30 min to 3 days.

133 ightly together into ordered stacks, whereas Abeta(1-42) forms short, crooked assemblies that knit to

134 in vitro resulted in decreased Abeta1-40 and Abeta1-42 fragments in a cell line model of Abeta produc

135 Single-CEL glycations at Lys-28 of Abeta1-42 had the least impact on fibril formation, wher

136 ouble-CEL glycations at Lys-16 and Lys-28 of Abeta1-42 had the most profound impact on the ability to

137 ucose, smaller hippocampal volume, lower CSF Abeta1-42, higher CSF total tau and phosphorylated tau18

138 rential neurotoxic effect of Abeta(1-40) and Abeta(1-42) in Alzheimer's disease.

139 We show that Abeta(1-42) in physiological concentrations acutely degr

140 creases with age, while the concentration of Abeta(1-42) in the cerebrospinal fluid (CSF) decreases i

141 By increasing the concentration of Abeta(1-42) in the sample, Abeta(1-42) octamers are also

142 soluble and detergent-insoluble Abeta1-40 or Abeta1-42 in brain homogenates did not reveal significan

143 de treatments increase the concentrations of Abeta1-42 in cerebral spinal fluid (CSF).

144 pal microglia activation, in the presence of Abeta1-42 in excess, produces neurotoxic and oligodendro

145 tf4 siRNA into the DG reduced the effects of Abeta1-42 in the forebrain.

146 mography [PET] and cerebrospinal fluid [CSF] Abeta1-42 ) in normal aging and dementia in a large mult

147 accumulation of amyloid beta peptide(1-42) (Abeta(1-42)) in extracellular plaques is one of the path

148 We show that Abeta(1-42) indeed oligomerizes over time in the micella

149 nversely, knockdown of 7B2 by RNAi increased Abeta(1-42)-induced cytotoxicity.

150 trated in vivo neuroprotection by decreasing Abeta1-42-induced toxicity by attenuating abnormal level

151 ty to decipher the mechanisms that accompany Abeta1-42-induced toxicity leading to neurodegeneration.

152 ergistic interaction likely results from the Abeta1-42-induced upregulation of the BDNF pro-domain re

153 ptic dysfunction, but we recently found that Abeta(1-42) inhibits the microtubule motor protein Eg5/k

154 We found that locally applied Abeta1-42 initiates axonal synthesis of a defined set of

155 ic mapping (SPM) for comparison of USPIO-PEG-Abeta1-42 injected AD transgenic and USPIO alone injecte

156 nal differences seen by VBA in the USPIO-PEG-Abeta1-42 injected AD transgenic correlated with the amy

157 Abeta1-42 injection into the dentate gyrus (DG) of mice

158 Abeta1-42 is involved in Alzheimer's disease (AD) pathog

159 ium extend to the C-terminal residues in the Abeta(1-42) isoform but not in Abeta(1-40).

160 animal model system we demonstrate that only Abeta1-42 leads to memory deficits.

161 An association was found between Abeta1-42 level and a single-nucleotide polymorphism in

162 itudinal increase in NMS with lower baseline Abeta1-42 level is an important finding that will have t

163 ixty-seven per cent of the patients with low Abeta(1-42) levels at baseline and normal cognition deve

164 gression revealed that patients with low CSF Abeta(1-42) levels at baseline developed cognitive impai

165 Patients with PD with low CSF Abeta(1-42) levels at baseline were more often cognitive

166 erse correlations between the plasma and CSF Abeta(1-42) levels until plaques form in transgenic mice

167 ssociated with tau pathology, independent of Abeta(1-42) levels, only in APOE epsilon4 negative parti

168 of patients having intermediate and high CSF Abeta(1-42) levels.

169 red than patients with intermediate and high Abeta(1-42) levels.

170 he gene most strongly associated with plasma Abeta1-42 levels (cortexin 3, CTXN3) on APP metabolism i

171 l individuals by significantly higher plasma Abeta1-42 levels (mean [SD]: carriers, 18.8 [5.1] pg/mL

172 Higher blood Abeta1-42 levels (P = 0.01) and higher Abeta42:40 ratio

173 here was no association between longitudinal Abeta1-42 levels and standardized uptake value ratios du

174 Plasma Abeta1-42 levels are higher in individuals who have seve

175 flickering regime that reduced Abeta1-40 and Abeta1-42 levels in the visual cortex of pre-depositing

176 he core structure of mature plaques, whereas Abeta1-42 localizes to diffuse amyloid aggregates.

177 eric Abeta1-42 (oAbeta1-42) and/or monomeric Abeta1-42 (mAbeta1-42) baits.

178 Here we show that the amyloid-beta peptide Abeta1-42 markedly prolongs the extracellular lifetime o

179 ies have suggested that cellular reuptake of Abeta(1-42) may be a crucial step in its cytotoxicity, b

180 Therapeutic reduction of HMW-Abeta(1-42) may prevent AD progression by ameliorating d

181 ta (Abeta) peptides (i.e., Abeta(1-40) , and Abeta(1-42) ) measured in serum.

182 We used concurrent cerebrospinal fluid Abeta1-42 measurements to identify subgroups of ADNI sub

183 2 years, including 150 participants with CSF Abeta1-42 measurements).

184 and phosphorylated tau181, and higher plasma Abeta1-42 measurements.

185 of alpha4beta2 nAChRs dramatically enhanced Abeta(1-42)-mediated increases in reactive oxygen specie

186 ron cultures and that miR-188-5p rescued the Abeta1-42-mediated synapse elimination and synaptic dysf

187 Treatment with either Abeta1-42 monomer or Abeta1-42 fibrils did not induce se

188 binding from internalization, we found that Abeta(1-42) monomers bound rapidly to the plasma membran

189 controls, we used no peptide treatment, 5 uM Abeta1-42 monomers, and 5 uM Abeta1-42 fibrils, respecti

190 These USPIO-PEG-Abeta1-42 nanoparticles were injected intravenously in A

191 a1-42-positive individuals but not among CSF Abeta1-42-negative individuals.

192 protein receptors on macrophages and reduces Abeta1-42 neurotoxicity.

193 At concentrations that impaired LTP, neither Abeta(1-42) nor monastrol inhibited NMDAR synaptic respo

194 human brain extract that bind to oligomeric Abeta1-42 (oAbeta1-42) and/or monomeric Abeta1-42 (mAbet

195 concentration of Abeta(1-42) in the sample, Abeta(1-42) octamers are also formed, made by two Abeta(

196 ured in vitro-derived distinct Abeta1-40 and Abeta1-42 oligomer size distributions and predicted that

197 ly reduced induction of senescence following Abeta1-42 oligomer treatment.

198 th factor receptor (VEGFR) expression in the Abeta1-42 oligomer-treated ECs, and these cells showed s

199 Distinct intermolecular arrangements between Abeta(1-42) oligomers and fibrils may explain why this o

200 uctural similarities and differences between Abeta(1-42) oligomers and fibrils suggest that folded be

201 ost prominent structural differences between Abeta(1-42) oligomers and fibrils were observed through

202 e potentially triggered and involve signals (Abeta(1-42) oligomers and HMGB-1) and pathways (RAGE/NF-

203 NMR experiments on Abeta(1-42) oligomers reveal chemical shifts of labeled

204 rted a stable and homogeneous preparation of Abeta(1-42) oligomers that has been characterized by var

205 Specifically, 150-kDa Abeta(1-42) oligomers with uniform (13)C and (15)N isoto

206 n channel conductance results suggested that Abeta(1-42) oligomers, but not monomers and fibers, form

207 e also of lower oligomeric state compared to Abeta(1-42) oligomers.

208 in microvascular ECs and HUVECs with high MW Abeta1-42 oligomers (5 uM, for 72 h).

209 Abeta1-42 oligomers also increased matrix metalloprotein

210 omers might be less toxic than Abeta1-40 and Abeta1-42 oligomers and offer a plausible explanation fo

211 ain endothelial cells (ECs) exposed to toxic Abeta1-42 oligomers can readily enter a senescence pheno

212 Interestingly, BCSFB disruption induced by Abeta1-42 oligomers did not occur in the presence of a b

213 tributions and predicted that the more toxic Abeta1-42 oligomers had more flexible and solvent-expose

214 Moreover, while Abeta1-42 oligomers impact on synaptic function, vAbeta1

215 that Alzheimer's disease-associated soluble Abeta1-42 oligomers induce BCSFB dysfunction and suggest

216 Intracerebroventricular injection of Abeta1-42 oligomers into the cerebral ventricles of mice

217 Our studies show that exposure to Abeta1-42 oligomers may impair vascular functions by alt

218 Brain ECs treated with Abeta1-42 oligomers showed increased senescence-associat

219 erebrocortical cultures, we demonstrate that Abeta1-42 oligomers trigger a dramatic increase in intra

220 In addition, NTR1 reversed Abeta1-42 oligomers-induced impairments in long term pot

221 e essential for the BCSFB leakage induced by Abeta1-42 oligomers.

222 r ability to produce toxic amyloid beta1-42 (Abeta1-42 ) oligomers from aggregated or soluble substra

223 rthermore, we showed that beta-amyloid 1-42 (Abeta(1-42)) oligomers, but not monomers and fibrils, an

224 nt interaction between CSF clusterin and CSF Abeta1-42 on the entorhinal cortex atrophy rate but not

225 48 hours of treatment with either 0.5-1.0muM Abeta(1-42) or 1-5muM monastrol reduced the dendritic sp

226 In addition, 1 nM Abeta(1-42) or 50 nM monastrol inhibited LTP #x223c;50%,

227 sponses on subsequent acute stimulation with Abeta(1-42) or nicotine, paralleled by increased express

228 age-associated findings were seen in plasma Abeta1-42 or Abeta1-40.

229 eater levels than worms harboring either the Abeta1-42 or tau transgene alone and interestingly witho

230 neurons at significantly higher levels than Abeta(1-42) over extended incubations.

231 d toxicity by attenuating abnormal levels of Abeta1-42, p-Tau, cleaved caspase-3, and cleaved PARP pr

232 e and increased tau pathology independent of Abeta(1-42) pathology.

233 n of binary and ternary complexes among TTR, Abeta(1-42) peptide, and TTR stabilizers using isotherma

234 analysis reveals time-dependent increases in Abeta1-42 peptide aggregation.

235 habditis elegans model expressing both human Abeta1-42 peptide and human tau protein pan-neuronally.

236 SPIO) nanoparticles, chemically coupled with Abeta1-42 peptide to image amyloid plaque deposition in

237 Microglial uptake of the mutant Abeta(1-42) peptides correlated with their aggregation l

238 s spectrometry approach and demonstrate that Abeta(1-42) peptides form coclusters with membrane mimet

239 tion (A673V), corresponding to position 2 of Abeta1-42 peptides (Abeta1-42A2V), that caused an early

240 an descent and for whom plasma Abeta1-40 and Abeta1-42 peptides levels had been quantified.

241 unctions under AD context, as it facilitated Abeta(1-42) phagocytosis and inhibited Abeta(1-42)-trigg

242 The hypothesis of this study was that active Abeta1-42 phagocytosis by macrophages prevents brain amy

243 and proresolution markers CD163+CD206], and Abeta1-42 phagocytosis in patients initially diagnosed a

244 Abeta1-42 phagocytosis increased in both ApoE groups (P

245 lon3/epsilon4 groups was 26.0 and macrophage Abeta1-42 phagocytosis was defective.

246 es in the higher range compared with the CSF Abeta1-42 plateau explained the differences in correlati

247 Amyloid beta1-42 (Abeta1-42) plays a central role in Alzheimer's disease.

248 The middle domain of Abeta1-42 plays a major role in aggregation, whereas the

249 the entorhinal cortex atrophy rate among CSF Abeta1-42-positive individuals but not among CSF Abeta1-

250 We show that these deficits depend on Abeta1-42 production and are prevented by tau reduction.

251 Two PSEN1 variants altered Abeta1-42 production from Abeta1-51 but not Abeta1-49.

252 ctive regions exposed on nuclei/oligomers of Abeta1-42, providing a molecular basis for the neuroprot

253 long, but a large body of evidence points to Abeta(1-42) rather than Abeta(1-40) as the cytotoxic for

254 ter improvements in memory and the sAPPalpha/Abeta1-42 ratio.

255 immunoassays, and tTau/Abeta(1-42) and pTau/Abeta(1-42) ratios calculated.

256 Performance of Tau/Abeta(1-42) ratios was superior to single biomarkers, an

257 p, they were elevated in subjects with T-tau/Abeta1-42 ratios greater than a cutoff that distinguishe

258 ed elevated SDS-stable, endogenous Abeta and Abeta1-42 relative to wild-type littermates, whereas 5XF

259 40 and 42 amino acids, denoted Abeta1-40 and Abeta1-42, respectively.

260 2.43, 95% CI=1.70 to 3.48), abnormal CSF tau/Abeta1-42 (RR=3.77, 95% CI=2.34 to 6.09), hippocampal at

261 T scan and at least 1 CSF beta-amyloid 1-42 (Abeta1-42) sample obtained within 30 days of each other

262 The values of the CSF Abeta1-42 samples and florbetapir-PET scans showed a non

263 d that the gene protein was able to modulate Abeta1-42 secretion.

264 ly between Abeta(1-42) and Abeta(1-40), with Abeta(1-42) showing a greater oligomerization propensity

265 amounts and interconversion of the dominant Abeta1-42 species.

266 re measured by INNO-BIA AlzBio3 immunoassay (Abeta1-42, T-tau, and P-tau181; Innogenetics Inc) or by

267 Slightly, but significantly, lower levels of Abeta1-42, T-tau, P-tau181, alpha-synuclein, and T-tau/A

268 study subjects,we found that measures of CSF Abeta1-42, T-tau, P-tau181, and alpha-synuclein have pro

269 a membrane mimicking environment, namely an Abeta(1-42) tetramer, which comprises a six stranded bet

270 Notably, Abeta(1-42) tetramers and octamers inserted into lipid b

271 (1-42) octamers are also formed, made by two Abeta(1-42) tetramers facing each other forming a beta-s

272 HSA affinity of Abeta monomers is lower for Abeta(1-42) than for Abeta(1-40).

273 Abeta1-51 resulted in much higher levels of Abeta1-42 than any other long Abeta peptides, but the pr

274 otein-protein interaction of Abeta(1-40) and Abeta(1-42) that is necessary for the formation of neuro

275 production of 150-kDa oligomeric samples of Abeta(1-42) (the 42-residue variant of the Abeta peptide

276 o predominant Abeta alloforms, Abeta1-40 and Abeta1-42, the latter is particularly strongly linked to

277 r the main putative AD pathogenic component, Abeta1-42, the PLL-UFM approach reveals the morphology o

278 Sustained exposure of Abeta(1-42) to alpha4beta2 nAChR-transfected cells for s

279 g neuronal cells were treated with nanomolar Abeta(1-42) to gain insights into the molecular mechanis

280 anding the aggregation of amyloid beta 1-42 (Abeta1-42) to give oligomers, protofibrils, and fibrils.

281 glucose, hippocampal gray matter volume, CSF Abeta1-42, total tau and phosphorylated tau181, and plas

282 ations of neurofilament light chain protein, Abeta1-42, total tau, phosphorylated tau, alpha-synuclei

283 e compounds totally suppress the toxicity of Abeta1-42 toward SH-SY5Y neuroblastoma cells, even at su

284 the effect of D-520 in a Drosophila model of Abeta(1-42) toxicity.

285 st, DNT1 mature-domain is protective against Abeta1-42 toxicity.

286 We found that oligomeric Abeta1-42 treatment diminished miR-188-5p expression in

287 tated Abeta(1-42) phagocytosis and inhibited Abeta(1-42)-triggered proinflammatory responses.

288 Abeta(1-42), tTau and pTau CSF concentrations were measu

289 -sheet-rich aggregates is a prerequisite for Abeta(1-42) uptake and cytotoxicity.

290 ip by rationally designing a variant form of Abeta1-42 (vAbeta1-42) differing in only two amino acids

291 Unlike Abeta1-42, we found that the variant does not self-assem

292 t levels of both soluble and insoluble brain Abeta(1-42) were reduced compared with those in AD(+) mi

293 The damaging effects of HMW-Abeta(1-42) were significantly greater than those of LMW

294 rs' geometry resulting from interaction with Abeta1-42 were also given by STD, trNOESY, and MM calcul

295 tau, phosphorylated tau 181 (P-tau181), and Abeta1-42 were available.

296 T-tau, P-tau181, alpha-synuclein, and T-tau/Abeta1-42 were seen in subjects with PD compared with he

297 n such as p-tau (PHF1), total ubiquitin, and Abeta1-42, when examined at 6 m after BCCAO.

298 wn about the structure of amyloid fibrils of Abeta1-42, which are considered the more toxic alloform

299 t prominent forms of Abeta are Abeta1-40 and Abeta1-42, which differ by two amino acids (I and A) at

300 ommonly used for the unspecific glycation of Abeta1-42, which results in a complex mixture of AGE-mod