The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity.
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The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathwayNeurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratioInteraction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancementTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesThe Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's DiseaseAmyloid-beta isoform metabolism quantitation by stable isotope-labeled kineticsRecent progress in understanding Alzheimer's β-amyloid structures.Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity.A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modelingAlzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Gender- and age-dependent gamma-secretase activity in mouse brain and its implication in sporadic Alzheimer disease.Distinct cerebrospinal fluid amyloid beta peptide signatures in sporadic and PSEN1 A431E-associated familial Alzheimer's disease.Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicityAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Substoichiometric inhibition of Abeta(1-40) aggregation by a tandem Abeta(40-1-Gly8-1-40) peptide.Identification of novel γ-secretase-associated proteins in detergent-resistant membranes from brain.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Critique of the use of fluorescence-based reporters in Escherichia coli as a screening tool for the identification of peptide inhibitors of Aβ42 aggregation.The pathogenic aβ43 is enriched in familial and sporadic Alzheimer diseaseAbeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species.Insight into amyloid structure using chemical probes.Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.Structural differences of amyloid-β fibrils revealed by antibodies from phage displayStructural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease.Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's DiseaseDiscovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formationBis(sulfosuccinimidyl) suberate (BS3) crosslinking analysis of the behavior of amyloid-β peptide in solution and in phospholipid membranes.The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein.Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processesFibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death.Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures.Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrilsAmyloid beta protein: Abeta40 inhibits Abeta42 oligomerization.Interrelationship between changes in the amyloid β 42/40 ratio and presenilin 1 conformationAmyloid-beta oligomers set fire to inflammasomes and induce Alzheimer's pathology.AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Active duty service members who sustain a traumatic brain injury have chronically elevated peripheral concentrations of Aβ40 and lower ratios of Aβ42/40.
P2860
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P2860
The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@en
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@nl
type
label
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@en
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@nl
prefLabel
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@en
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@nl
P2860
P50
P356
P1476
The ratio of monomeric to aggr ...... fibrillogenesis, and toxicity.
@en
P2093
P2860
P304
28176-28189
P356
10.1074/JBC.M803159200
P407
P577
2008-08-11T00:00:00Z