ライフサイエンスコーパス: Abeta42

1 nucleation of the 42-residue form of Abeta (Abeta42).

2 shed day/night amplitude of both Abeta40 and Abeta42.

3 ion of toxic oligomers formed from natural l-Abeta42.

4 s of the peptide, Abeta40 and the more toxic Abeta42.

5 istic systems such as the STVIIE peptide and Abeta42.

6 ly high structural similarity with wild-type Abeta42.

7 ikely to favorably impact the aggregation of Abeta42.

8 uct fibrils is influenced by the presence of Abeta42.

9 43 spontaneously aggregates more slowly than Abeta42.

10 dy the two major Abeta variants, Abeta40 and Abeta42.

11 ts SIRT6 reduction and DNA damage induced by Abeta42.

12 nm Abeta40, Abeta40, aggregated Abeta40, and Abeta42.

13 te complexity and loss of neurites caused by Abeta42.

14 subsequently convert to having abnormal CSF Abeta42.

15 lasma from wild-type mice i.v. injected with Abeta42.

16 ta42, t-tau, p-tau, t-tau/Abeta42, and p-tau/Abeta42.

17 in CsgC client proteins that is not found in Abeta42.

18 patient groups (all P < .001), but not with Abeta42.

19 se with their previously reported effects on Abeta42.

20 es, but a significant reduction of insoluble Abeta42.

21 of neurotoxic species during aggregation of Abeta42.

22 in the mature Abeta40 aggregates, but not in Abeta42.

23 ms and also to the increased cytotoxicity of Abeta42.

24 eptides could attenuate the toxic effects of Abeta42.

25 ence in the effects of Zn(+2) on Abeta40 and Abeta42.

26 001), P-tau (1.88, 1.79-1.97, p<0.0001), and Abeta42 (0.56, 0.55-0.58, p<0.0001).

27 was also strong (average ratio 0.67 for CSF Abeta42, 1.72 for P-tau, and 1.76 for T-tau).

28 D of residuals: Abeta40, -7.42 pM; P < .001; Abeta42, -3.72 pM; P < .001).

29 conformation, and resulting increase in the Abeta42/40 ratio.

30 blood Abeta1-42 levels (P = 0.01) and higher Abeta42:40 ratio (P = 0.06) were observed in participant

31 these peptides, we expressed Abeta36-40 and Abeta42-43 in Drosophila melanogaster to evaluate inhere

32 des (Abeta37-39), and longer Abeta peptides (Abeta42-43).

33 performed with the full-size Abeta protein (Abeta42), a decapeptide Abeta(14-23) and alpha-synuclein

34 Abeta42, a major component of senile plaques, decreases

35 This is in agreement with the finding that Abeta42-A2V leads to early-onset Alzheimer's disease and

36 ply this work-flow to the disease-associated Abeta42-A2V variant, and to a variation in pH as example

37 NFL, NSE, VLP-1, and HFABP), APP metabolism (Abeta42, Abeta40, Abeta38, sAPPalpha, and sAPPbeta), tan

38 rains and reduced in KI/+ brains, though the Abeta42/Abeta40 ratio is slightly increased in KI/+ brai

39 ides produced by proteolysis, as well as the Abeta42/Abeta40 ratio, both of which are linked to the p

40 the newer assays improved significantly when Abeta42:Abeta40 (AUCs, 0.93-0.95; P </= .01), Abeta42 to

41 The concordance of CSF Abeta42 levels and Abeta42:Abeta40 and Abeta42:tau ratios with visual [18F]

42 suggest the benefit of implementing the CSF Abeta42:Abeta40 or Abeta42:tau ratios as a biomarker of

43 F]flutemetamol PET assessment when using the Abeta42:Abeta40 or Abeta42:tau ratios.

44 A combination of the Abeta42:Abeta40 ratio and T-tau or P-tau level did not i

45 Both in this Abeta42/Abeta43 co-aggregation reaction and in cross-see

46 by microglia are less compact but have high Abeta42 affinity, leading to the formation of protofibri

47 eads to compact plaque microregions with low Abeta42 affinity.

48 a qualitative difference between Abeta40 and Abeta42 aggregates in the brain tissue of patients with

49 blocked glial clearance of Abeta42 in vitro Abeta42 aggregates were colocalized with extracellular c

50 in catalyses the heterogeneous nucleation of Abeta42 aggregates.

51 We conducted in vitro assays to assess Abeta42 aggregation and glial clearance with and without

52 Soluble Abeta42 aggregation intermediates (oligomers) have emerg

53 synuclein that determines the outcome of the Abeta42 aggregation reaction.

54 p a rational drug discovery strategy against Abeta42 aggregation that uses as a read-out the changes

55 ds that target specific microscopic steps in Abeta42 aggregation.

56 for other therapeutic approaches to mitigate Abeta42 aggregation.

57 l molecules on specific microscopic steps in Abeta42 aggregation.

58 il-catalyzed secondary nucleation process in Abeta42 aggregation.

59 r species in Alzheimer's disease (AD) is the Abeta42 alloform of Abeta peptide, which is dominant in

60 eta42 and Abeta43 aggregate more slowly than Abeta42 alone.

61 ously reported effects of age and amyloid on Abeta42 amplitude at least partially affect each other.

62 ta43 fibrils are very inefficient at seeding Abeta42 amyloid formation, even though Abeta42 fibrils e

63 as a possible mechanism of cell toxicity of Abeta42 amyloids.

64 a higher (>50%) irreversible loss of soluble Abeta42 and a 10-fold higher Abeta42 reversible exchange

65 stic insight into the aggregation pathway of Abeta42 and a putative toxic mechanism in the pathogenes

66 Abeta42 and Abeta40 differ only near the C-terminus, whe

67 at low levels compared with the predominant Abeta42 and Abeta40 forms, but it has been suggested tha

68 We analyzed plasma levels of Abeta42 and Abeta40 in a cohort of 719 individuals (the

69 binant adeno-associated virus (AAV) encoding Abeta42 and Abeta40 peptides fused to BRI2 protein by in

70 h constructs leads to production of secreted Abeta42 and Abeta40 respectively.

71 ted with Alzheimer's disease, whereas plasma Abeta42 and Abeta40 were not.

72 Plasma levels of Abeta42 and Abeta40 were reduced in AD dementia compared

73 nd cerebrospinal fluid (CSF) levels for both Abeta42 and Abeta40, and negative correlations between p

74 Finally, mixtures of Abeta42 and Abeta43 aggregate more slowly than Abeta42 a

75 Here, we report that both Abeta42 and Abeta43 spontaneously aggregate into mature

76 elation (r = -0.879, p = 0.0001) between CSF Abeta42 and absolute (but subthreshold) PIB binding was

77 Furthermore, this peptide bound fibrillar Abeta42 and also stained plaques ex vivo in brain tissue

78 -derived exosomes accelerated aggregation of Abeta42 and blocked glial clearance of Abeta42 in vitro

79 We synthesized l- and D-Abeta42 and found their equimolar mixing to lead to acce

80 40, and negative correlations between plasma Abeta42 and neocortical amyloid deposition (measured wit

81 Still, Abeta42 and NTE-Abeta42 coaggregate to form mixed fibril

82 In addition, we computed t-tau/Abeta42 and p-tau/Abeta42 ratios.

83 mation, neuronal degeneration, sphingolipid, Abeta42 and phospho-tau levels, and memory-related behav

84 um anticeramide IgG, glial activation, total Abeta42 and plaque burden, tau phosphorylation, and impr

85 holinesterase in vitro and moderately potent Abeta42 and tau antiaggregating agents in a simple E. co

86 the aggregation of the beta-Amyloid Peptide Abeta42 and transthyretin.

87 cognitive impairment (age, UPSIT, RBDSQ, CSF Abeta42, and caudate uptake on DAT imaging) allowed pred

88 Due to their consistency, T-tau, P-tau, Abeta42, and NFL in CSF should be used in clinical pract

89 fluid levels of Abeta42, t-tau, p-tau, t-tau/Abeta42, and p-tau/Abeta42.

90 -2 and MMP-9 were incubated with Abeta40 and Abeta42, and the resulting proteolytic fragments were as

91 demonstrated to have high affinity to serum Abeta42, and to be able to identify AD sera with high se

92 Engineered anti-Abeta42 antibodies are a promising strategy to stall the

93 downstream of Draper in glia in response to Abeta42(arc) exposure.

94 Neuronal expression of human Abeta42(arc) in adult flies results in robust Abeta accu

95 As in the brain, Abeta40 and Abeta42 are present in the heart, and their expression i

96 ction and steady-state levels of Abeta40 and Abeta42 are undetectable in KI/KI brains and reduced in

97 2-residue amyloid-beta peptides (Abeta40 and Abeta42) are polymorphic, with variations in molecular s

98 We identified the central region of Abeta42 as the most critical region for the interaction,

99 fibrillization of beta-amyloid peptide 1-42 (Abeta42) as a function of time and by comparing to the r

100 andidate directly interacted with oligomeric Abeta42, as shown by coimmunoprecipitation and surface p

101 a40 aggregated into amyloid fibrils, whereas Abeta42 assembled into oligomers that inserted into lipi

102 ed with familial amyloid polyneuropathy, and Abeta42 associated with Alzheimer's disease by stabilizi

103 e protection of cells from the toxicity of l-Abeta42 at concentrations up to 50 mum.

104 se hippocampal neurons following exposure to Abeta42 at picomolar concentrations, mimicking its physi

105 eta [SE] = -0.02 [0.01], P = .02), and p-tau/Abeta42 (beta [SE] = -0.002 [0.001], P = .004).

106 u (beta [SE] = -0.71 [0.27], P = .01), t-tau/Abeta42 (beta [SE] = -0.02 [0.01], P = .02), and p-tau/A

107 -ray crystallographic analysis revealed that Abeta42 binding to fragment D of fibrinogen induced a st

108 la to investigate the protective activity of Abeta42-binding agents in an AD-relevant functional assa

109 peutics, reduce production of the pathogenic Abeta42 but increase the relative abundance of short Abe

110 d day/night amplitude and linear increase of Abeta42 but not of Abeta40.

111 bolites (secreted APPbeta, C99, Abeta40, and Abeta42) but has no effect on presenilin 1 and presenili

112 amyloid precursor protein APP, is related to Abeta42 by an additional Thr residue at the C-terminus.

113 studies indicate that treatments that lower Abeta42 by raising the levels of short Abeta peptides co

114 can only assume U-shaped conformations while Abeta42 can also arrange as S-shaped three-stranded chai

115 fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.

116 Still, Abeta42 and NTE-Abeta42 coaggregate to form mixed fibrils and fibrils of

117 t baseline exhibited significantly lower CSF Abeta42 compared to those who remained PIB-negative (n =

118 receptor as compared to ApoE4, regardless of Abeta42 concentration.

119 ignificantly stronger for the longer peptide Abeta42, correlating with its importance in AD pathology

120 kers of neurodegeneration (T-tau, P-tau, and Abeta42), CSF NFL, and plasma T-tau were strongly associ

121 is associated with premature loss of normal Abeta42 day/night patterns in older adults, suggesting t

122 rs of future Abeta positivity (levels of CSF Abeta42 declining below a previously validated cutoff le

123 ransgenic mice at levels sufficient to drive Abeta42 deposition, Abeta38 and Abeta40 did not deposit

124 Concentrations of CSF Abeta42 derived from the new immunoassays (modified INNO

125 Here we report fibril propagation of an Abeta42 dodecamer called large fatty acid-derived oligom

126 -INNOTEST (r = 0.97), Abeta42-FL (r = 0.93), Abeta42-EI (r = 0.93), and Abeta42-MSD (r = 0.95) assays

127 The mixing of Abeta42 enantiomers thus accelerates the formation of no

128 jor species of Abeta peptides, in particular Abeta42, exhibited a strong inhibitory effect on the pre

129 nteracting with the Abeta peptide to inhibit Abeta42 fiber formation.

130 on assays, antioxidant assays, and assays of Abeta42 fibrillation.

131 lations demonstrated that brazilin inhibited Abeta42 fibrillogenesis by directly binding to Abeta42 s

132 i) selection of scFvs with high affinity for Abeta42 fibrils after removal of scFvs that bind Abeta42

133 eding Abeta42 amyloid formation, even though Abeta42 fibrils efficiently seed amyloid formation by Ab

134 Data for Abeta42 fibrils indicate structural heterogeneity in mos

135 esonance (ssNMR) measurements on Abeta40 and Abeta42 fibrils prepared by seeded growth from extracts

136 We have found Abeta42 fibrils to exhibit stronger energies in inter-ch

137 n Abeta40 fibrils in alternative structures, Abeta42 fibrils, or amyloid fibrils formed from other se

138 rils have fewer strong backbone H-bonds than Abeta42 fibrils, some of which are lost at the C-terminu

139 aggregation reaction and in cross-seeding by Abeta42 fibrils, the structure of the Abeta43 in the pro

140 glutamine peptides and redirects assembly of Abeta42 fibrils.

141 e resulting candidate scFvs that bind to the Abeta42 fibrils; and (iii) kinetic screening and analysi

142 th the modified Abeta42-INNOTEST (r = 0.97), Abeta42-FL (r = 0.93), Abeta42-EI (r = 0.93), and Abeta4

143 Abeta42 forms oligomers and ultimately plaques, and it h

144 changes of the cytosolic side of TMD4 affect Abeta42-generating gamma-secretase activity.

145 We discovered that Abeta42 hexamers and dodecamers quickly become the domin

146 tical signature regions, cerebrospinal fluid Abeta42, hippocampal volume, and AD signature cortical t

147 s reduced leading to enlarged protofibrillar Abeta42 hotspots and more severe neuritic dystrophy.

148 , leading to the formation of protofibrillar Abeta42 hotspots that are associated with more severe ax

149 more apparent in at-risk epsilon4 carriers (Abeta42 in an allele dose-dependent manner) and appeared

150 Recently, we showed that abnormal levels of Abeta42 in cerebrospinal fluid (CSF) can be detected bef

151 cline induced by extracellular deposition of Abeta42 in Drosophila.

152 ly enhance accumulation of aggregation-prone Abeta42 in intracellular acidic compartments.

153 a42 fibrils after removal of scFvs that bind Abeta42 in its monomeric form; (ii) ranking, by surface

154 on average, 28% lower levels of Abeta40 and Abeta42 in plasma as compared to the controls and the ca

155 s already evident in individuals with normal Abeta42 in the CSF and normal amyloid PET who subsequent

156 prove memory performance in flies expressing Abeta42 in the mushroom body neurons, which are intimate

157 ta accumulation (2- and 3.5-fold increase in Abeta42 in the soluble and insoluble protein fractions,

158 on of Abeta42 and blocked glial clearance of Abeta42 in vitro Abeta42 aggregates were colocalized wit

159 disruption of actin cytoskeleton induced by Abeta42 in vitro was inhibited by bexarotene treatment.

160 sing substantial effects in both Abeta40 and Abeta42 include His14, Gln15, Ala30, Ile31, Met35, and V

161 , Leu17, and Asn 27, whereas sites unique to Abeta42 include Phe20 and Ala21.

162 ere is a strong negative correlation between Abeta42-induced DNA damage and p53 levels, a protein inv

163 ile plaques, decreases SIRT6 expression, and Abeta42-induced DNA damage is prevented by the overexpre

164 pendent SIRT6 expression protects cells from Abeta42-induced DNA damage, making SIRT6 a promising new

165 support the application of this paradigm of Abeta42-induced memory loss in Drosophila to investigate

166 Furthermore, Abeta42-induced upregulation of the phagolysosomal marke

167 showed higher correlations with the modified Abeta42-INNOTEST (r = 0.97), Abeta42-FL (r = 0.93), Abet

168 (r = 0.95) assays compared with the classic Abeta42-INNOTEST assay (r = 0.88; P </= .01).

169 However, the classic Abeta42-INNOTEST assay showed better concordance with vi

170 The signal in the classic Abeta42-INNOTEST assay was partly quenched by recombinan

171 However, in the presence of Abeta42, insulin failed to elicit a downstream response

172 tion, the aggregation free energy profile of Abeta42 is more downhill, with a computed solubility tha

173 However, Abeta42 is more neurotoxic and essential to the etiology

174 ithin the A2T-bound monomer, while A2V-bound Abeta42 is often enhanced in overall disorder.

175 Nascent Abeta42 is predominantly disordered but samples alpha-he

176 42-residue form of the amyloid-beta peptide (Abeta42) is a pivotal event in Alzheimer's disease (AD).

177 ing and cerebrospinal fluid (CSF) Abeta1-42 (Abeta42) is an early indicator of preclinical Alzheimer

178 A notable reorganization of the Abeta42 landscape is revealed due to hexapeptide associa

179 eta6 hexapeptide binding on the monomeric WT Abeta42 landscape.

180 The preprotofibrils are a single Abeta42 layer in height and can extend several hundred n

181 The concordance of CSF Abeta42 levels and Abeta42:Abeta40 and Abeta42:tau ratio

182 biogenesis and synaptic activity and reduces Abeta42 levels and protects AD neurons against Abeta-ind

183 CSF Abeta42 levels are tightly coupled with cortical amyloid

184 All participants had normal CSF Abeta42 levels at baseline.

185 GSM treatment selectively reduced endogenous Abeta42 levels by approximately 80%.

186 Patients with abnomal CSF p-tau and Abeta42 levels exhibited both reduced and increased func

187 Baseline CSF Abeta42 levels in the lower part of the reference range

188 To determine the concordance between CSF Abeta42 levels measured using 5 different immunoassays a

189 arly as early middle age (P </= .05) and low Abeta42 levels were associated with the development of c

190 Similarly, Abeta42 levels were increased by 69% (p < 0.001) in the

191 Abeta42 levels were significantly reduced in DDQ-treated

192 F VILIP-1, tau, and p-tau181 levels (but not Abeta42 levels) predicted rates of whole-brain and regio

193 for Abeta accumulation as defined by low CSF Abeta42 levels.

194 The agreement between CSF Abeta42 measures from different immunoassays and visual

195 that the fibril core consists of a dimer of Abeta42 molecules, each containing four beta-strands in

196 Concurrently, Abeta6-bound Abeta42 monomer exhibits alternative structural features

197 of the N-terminal hexapeptide binding on the Abeta42 monomer structure, which might help in explainin

198 42-FL (r = 0.93), Abeta42-EI (r = 0.93), and Abeta42-MSD (r = 0.95) assays compared with the classic

199 ositive (Abeta+) AD from cerebrospinal fluid Abeta42-negative (Abeta-) CN participants.

200 Thus, the holdase activity of secHsp70 masks Abeta42 neurotoxicity by promoting the accumulation of n

201 secreted form of Hsp70 (secHsp70) suppresses Abeta42 neurotoxicity in adult eyes, reduces cell death,

202 ed Drosophila to explore a strategy to block Abeta42 neurotoxicity through engineering of the Heat sh

203 roinflammatory response and beta-amyloid 42 (Abeta42) neurotoxicity independent of traditional circul

204 ement that we named beta-barrel pore-forming Abeta42 oligomers (betaPFOsAbeta42).

205 een developed to efficiently eliminate toxic Abeta42 oligomers as a promising treatment strategy for

206 solvent-exposure of hydrophobic residues in Abeta42 oligomers contributes to the different aggregati

207 Picomolar concentrations of Abeta42 oligomers could be observed to induce Ca(2+) inf

208 s candidate reduced the formation of soluble Abeta42 oligomers, with the concurrent generation of non

209 to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monom

210 However, in AD cases, Abeta42 pathology might be associated with WML, especial

211 ar behavior is observed for oligomers of the Abeta42 peptide associated with Alzheimer's disease.

212 onformational folding avenues sampled by the Abeta42 peptide owing to the presence of its two extra r

213 inserted at the edges of a large hydrophobic Abeta42 peptide segment (Abeta residues 17-42) in CDR3 o

214 Abundant proteins of the Abeta42 peptide-generating system in ADEs may sustain le

215 d stability and affinity for the Alzheimer's Abeta42 peptide.

216 of soluble assemblies of the amyloid-beta42 (Abeta42) peptide.

217 We show that this allows Abeta42 peptides to assemble pore-like structures that m

218 ed to the increased aggregation stability of Abeta42 peptides which possess two extra residues (Ile 4

219 ormation of a tetramer unit by four separate Abeta42 peptides.

220 ly relationships of 76 different Abeta40 and Abeta42 peptides.

221 gonist, and this partial rescue of microglia Abeta42 phagocytosis was largely mediated by CD36 activi

222 ue form of the amyloid beta-protein (Abeta), Abeta42, play a critical role in the etiology of Alzheim

223 e regions best separated cerebrospinal fluid Abeta42-positive (Abeta+) AD from cerebrospinal fluid Ab

224 between the cytosolic sides of TMD4/TMD7 and Abeta42 production levels, suggesting that allosteric co

225 Similar to Abeta40 and Abeta42, production of Abeta43 is undetectable in KI/KI

226 Interestingly, NUCB1 prevents Abeta42 protofibril toxicity in a cellular assay.

227 ddition, we computed t-tau/Abeta42 and p-tau/Abeta42 ratios.

228 peptoid nanosheet containing surface-exposed Abeta42-recognizing loops is constructed, and a label-fr

229 This lead compound demonstrated robust Abeta42 reductions and subsequent Abeta37 increases in b

230 dues 16-21 and 29-36 that is dominant in the Abeta42 reference ensemble.

231 ngly stabilize the oligomeric structures for Abeta42 relative to Abeta40, and greatly facilitate the

232 ases, result in an increase in the amount of Abeta42 relative to Abeta40.

233 Because Abeta42, relative to Abeta40, has a more prominent role

234 re it is shown that the data for Abeta40 and Abeta42 require that the nuclei be monomeric; that is, a

235 e that overexpression of secreted Abeta40 or Abeta42 resulted in dramatic induction of drusen-like de

236 loss of soluble Abeta42 and a 10-fold higher Abeta42 reversible exchange rate.

237 are variants (E270K and T947M) and increased Abeta42 secretion for the common variant (A528T).

238 cted cell lines showed increased Abeta40 and Abeta42 secretion for the rare variants (E270K and T947M

239 y 293 cell lines were tested for Abeta40 and Abeta42 secretion, and the amount of the amyloid precurs

240 in turn can result in increased Abeta40 and Abeta42 secretion.

241 thesized that the addition of mirror-image d-Abeta42 should reduce the concentration of toxic oligome

242 ed detergent micelle conditions, Abeta40 and Abeta42 showed different behavior.

243 enzyme 1 (BACE-1), gamma-secretase, soluble Abeta42, soluble amyloid precursor protein (sAPP)beta, s

244 eta42 fibrillogenesis by directly binding to Abeta42 species via hydrophobic interactions and hydroge

245 d ability to target monomeric and aggregated Abeta42 species, this candidate holds promise for novel

246 sponse was achieved with a downregulation of Abeta42-specific effector (Th1, Th17, and Th2) cell resp

247 dran angle values in certain residues of the Abeta42 strain compared to Abeta40.

248 population shift in a subset of the original Abeta42 structural sub-populations, including a sevenfol

249 Abeta40 aggregation landscape disappears for Abeta42, suggesting that the Abeta42 tetramer has a more

250 rs for the diagnosis of Alzheimer's disease (Abeta42, T-tau, and P-tau) have been assessed in numerou

251 Cerebrospinal fluid levels of Abeta42, t-tau, p-tau, t-tau/Abeta42, and p-tau/Abeta42.

252 t of implementing the CSF Abeta42:Abeta40 or Abeta42:tau ratios as a biomarker of amyloid deposition

253 f CSF Abeta42 levels and Abeta42:Abeta40 and Abeta42:tau ratios with visual [18F]flutemetamol PET sta

254 assessment when using the Abeta42:Abeta40 or Abeta42:tau ratios.

255 disappears for Abeta42, suggesting that the Abeta42 tetramer has a more diverse structural range.

256 The Abeta42 tetramer unit that formed in the initial simulat

257 Abeta42 tetramers adopted an oblate ellipsoid shape and

258 ctly image populations of small oligomers of Abeta42 that occur at the earliest stages of aggregation

259 in blocks the autocatalytic proliferation of Abeta42 (the 42-residue form of Abeta) fibrils, fibrilla

260 In contrast to Abeta42, the short Abeta peptides were not toxic and, wh

261 SecHsp70 binding to Abeta42 through its holdase domain is neuroprotective, b

262 uggests the mechanisms by which the ratio of Abeta42 to Abeta40 can affect cell toxicity.

263 An increased ratio of Abeta42 to Abeta40 raises the fraction of oligomers cont

264 ominent role in AD, the higher propensity of Abeta42 to form betaPFOs constitutes an indication of th

265 otal tau (T-tau) (AUCs, 0.94; P </= .05), or Abeta42 to phosphorylated tau (P-tau) (AUCs, 0.94-0.95;

266 (scFv9) and C-terminal (scFv42.2) regions of Abeta42 to suppress the progressive memory decline induc

267 Baseline age, MoCA and UPSIT scores, and CSF Abeta42 to t-tau ratio were associated with MoCA score a

268 ibrillization leads to reduced adsorption of Abeta42 to the nanoparticles increasing the TR-LRET sign

269 beta42:Abeta40 (AUCs, 0.93-0.95; P </= .01), Abeta42 to total tau (T-tau) (AUCs, 0.94; P </= .05), or

270 uctural ensembles of the IDP amyloid-beta42 (Abeta42) to an alternative sequence in which a nitroxide

271 nventory Test (UPSIT) scores, CSF amyloid - (Abeta42) to t-tau ratio, and APOE status were associated

272 taneous overexpression of BRI-Abeta40 or BRI-Abeta42 together resulted in dose-dependent and cumulati

273 re for collection of CSF samples, from which Abeta42, total tau (t-tau), and phosphorylated tau (p-ta

274 Changes in Abeta40, Abeta42, total tau, P-tau181, VILIP-1, and YKL-40 and, i

275 toxicity and potential modulatory effects on Abeta42 toxicity.

276 These lipoproteins facilitate Abeta42 transport more efficiently than Abeta40, consist

277 regation in three unrelated amyloid species: Abeta42, transthyretin, and human islet amylin polypepti

278 ation of its two major isoforms, Abeta40 and Abeta42, using a statistical mechanical modelling approa

279 been Abeta-reducing therapies including DNA Abeta42 vaccination as a promising approach to delay or

280 DNA Abeta42 vaccination upregulated T regulator cells (CD4+,

281 With DNA Abeta42 vaccination, a Th2-type noninflammatory immune r

282 heimer disease (AD) and DNA amyloid beta 42 (Abeta42) vaccination as a potential therapy.

283 The mass spectrometry-derived Abeta42 values showed higher correlations with the modif

284 escence to study the aggregation kinetics of Abeta42 variants with N-terminal extensions of 5-40 resi

285 with regional WML in all regions, while CSF Abeta42 was associated with temporal WML only.

286 ntrols, SCD and MCI) plasma concentration of Abeta42 was just moderately decreased whereas Abeta40 le

287 nhanced fibril formation propensity, racemic Abeta42 was less prone to form soluble oligomers.

288 ur experiments revealed that the assembly of Abeta42 was more sensitive to chiral substitutions than

289 ts protective activity against extracellular Abeta42, we added a signal peptide to Hsp70.

290 subsequent oligomer-membrane interactions of Abeta42, we performed atomistic molecular-dynamics (MD)

291 Levels of CSF Abeta42 were analyzed using the classic INNOTEST and the

292 in all subgroups, while lower levels of CSF Abeta42 were associated with WML mainly in AD.

293 The amplitude and linear rise of Abeta42 were both associated with turnover (r = -0.38; P

294 e was performed, and kinetics of Abeta40 and Abeta42 were measured.

295 0 (P = .001-.97), longitudinal reductions in Abeta42 were observed in some individuals as early as ea

296 es were not toxic and, when coexpressed with Abeta42, were protective in a dose-dependent fashion.

297 o be more vertical along the fibril axis for Abeta42 which thus reduces the inter-atomic distance bet

298 tease that produces amyloid-beta peptide 42 (Abeta42), which is the toxic and aggregation-prone speci

299 raises the fraction of oligomers containing Abeta42, which can increase the hydrophobicity of the ol

300 lations, elucidating preferential binding of Abeta42 with the A2V and A2T hexapeptides compared to WT