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Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils
TLDR
It is shown that low-temperature and low-salt conditions can stabilize disc-shaped oligomers (pentamers) that are substantially more toxic to mouse cortical neurons than protofibrils and fibrils, and that these neurotoxic oligomers do not have the β-sheet structure characteristic of fibril. Expand
LRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms
TLDR
Low-affinity LRP/Aβ interaction and/or Aβ-induced LRP loss at the BBB mediate brain accumulation of neurotoxic Aβ in transgenic mice and patients with cerebrovascular β-amyloidosis. Expand
LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms.
TLDR
Low-affinity LRP/Abeta interaction and/or Abeta-induced LRP loss at the BBB mediate brain accumulation of neurotoxic Abeta, consistent with reduced brain capillary LRP levels in Abetas transgenic mice, AD, and patients with cerebrovascular beta-amyloidosis. Expand
Early-onset and Robust Cerebral Microvascular Accumulation of Amyloid β-Protein in Transgenic Mice Expressing Low Levels of a Vasculotropic Dutch/Iowa Mutant Form of Amyloid β-Protein Precursor*
TLDR
It is shown that overexpression of human AβPP is not required for early-onset and robust accumulation of both vascular and parenchymal Aβ in mouse brain, and in vivo transport studies demonstrated that Dutch/Iowa mutant Aβ was more readily retained in the brain compared with wild-type Aβ. Expand
Cerebral microvascular amyloid beta protein deposition induces vascular degeneration and neuroinflammation in transgenic mice expressing human vasculotropic mutant amyloid beta precursor protein.
TLDR
The Tg-SwDI mouse is identified as a unique model to investigate selective accumulation of cerebral microvascular amyloid and the associated neuroinflammation in Alzheimer's disease and related disorders. Expand
Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity*
TLDR
The results suggest that the ability of non-fibrillar Aβ oligomers to interact with and disrupt cellular membranes is linked to the degree of solvent exposure of their central and C-terminal hydrophobic peptide segments. Expand
The effects of NOS2 gene deletion on mice expressing mutated human AbetaPP.
TLDR
It is hypothesized that during long-term exposure to amyloid-beta (Abeta) in Alzheimer's disease (AD), NO levels fall in the brain to a threshold at which the protective effects of NO cannot be sustained, promoting Abeta mediated damage. Expand
Localization of a Fibrillar Amyloid β-Protein Binding Domain on Its Precursor*
TLDR
It is concluded that His110, Val112, and Ile113, residing in a common β-strand region within A βPP-(18–119), comprise a domain that mediates the binding of AβPP to fibrillar peptides. Expand
Progression of Amyloid Pathology to Alzheimer's Disease Pathology in an Amyloid Precursor Protein Transgenic Mouse Model by Removal of Nitric Oxide Synthase 2
TLDR
Removing NOS2 from an APP transgenic mouse results in development of a much greater spectrum of AD-like pathology and behavioral impairments, and Neuropeptide Y neurons appear to be particularly vulnerable in the APPSwDI/NOS2−/− mice. Expand
Amyloid Reduction by Amyloid-β Vaccination Also Reduces Mouse Tau Pathology and Protects from Neuron Loss in Two Mouse Models of Alzheimer's Disease
TLDR
By providing evidence that reducing amyloid pathology also reduces nonmutant tau pathology and blocks neuron loss, these data support the development of amyloids-lowering therapies for disease-modifying treatment of AD. Expand
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