Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates.
Dominic M. Walsh,Dean M. Hartley,Yoko Kusumoto,Youcef Fezoui,Margaret M. Condron,Aleksey Lomakin,Aleksey Lomakin,George B. Benedek,Dennis J. Selkoe,David B. Teplow +9 more
TL;DR: Walsh et al. as discussed by the authors found that amyloid protofibrils are in equilibrium with low molecular weight Abeta (monomeric or dimeric) and have a secondary structure characteristic of Amyloid fibrils.
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About: This article is published in Journal of Biological Chemistry. The article was published on 03 Sep 1999. and is currently open access. The article focuses on the topics: Amyloid beta & P3 peptide.
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Citations
Protein Misfolding, Functional Amyloid, and Human Disease
TL;DR: The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide.
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TL;DR: Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.
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Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo.
Dominic M. Walsh,Igor Klyubin,Julia V. Fadeeva,William K. Cullen,Roger Anwyl,Michael S. Wolfe,Michael J. Rowan,Dennis J. Selkoe +7 more
TL;DR: It is reported that natural oligomers of human Aβ are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell, indicating that synaptotoxic Aβ oligomers can be targeted therapeutically.
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
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TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.
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A beta oligomers - a decade of discovery.
TL;DR: Accumulating evidence suggests that soluble forms of Aβ are indeed the proximate effectors of synapse loss and neuronal injury in Alzheimer’s disease.
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References
Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity.
TL;DR: This article showed that microinjection of plaque-equivalent concentrations of fibrillar, but not soluble, Abeta in the aged rhesus monkey cerebral cortex results in profound neuronal loss, tau phosphorylation and microglial proliferation.
Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
TL;DR: Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length.
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
TL;DR: Alternative enzymatic processing of beta-APP liberates A beta, which has a propensity to form amyloid fibrils; A beta can damage and kill neurons and increase their vulnerability to excitotoxicity.
Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay.
TL;DR: In this article, the authors modify the original CR-insulin method for quantifying Abeta aggregation and discuss the reasons why application of the original method is not valid for this purpose.
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