ライフサイエンスコーパス: Abeta(1-42)

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

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

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

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

5 Abeta1-42 oligomers also increased matrix metalloprotein

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

7 48 hours of treatment with either 0.5-1.0muM Abeta(1-42) or 1-5muM monastrol reduced the dendritic sp

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

93 2 years, including 150 participants with CSF Abeta1-42 measurements).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

152 X3 silencing caused an earlier activation of Abeta(1-42)-induced caspase-12.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

251 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

283 (1-42) octamers are also formed, made by two Abeta(1-42) tetramers facing each other forming a beta-s

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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