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.
Christian Haass,Dennis J. Selkoe +1 more
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.
Monica Bucciantini,Elisa Giannoni,Fabrizio Chiti,Fabrizio Chiti,Fabiana Baroni,Lucia Formigli,Jesús Zurdo,Niccolò Taddei,Giampietro Ramponi,Christopher M. Dobson,Massimo Stefani +10 more
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
Spectroscopic characterization of conformational differences between PrPC and PrPSc: an alpha-helix to beta-sheet transition.
Michael A. Baldwin,Keh-Ming Pan,Jack T. Nguyen,Ziwei Huang,Darlene Groth,Ana Serban,María Gasset,Ingrid Mehlhorn,Robert J. Fletterick,Fred E. Cohen,Stanley B. Prusiner +10 more
TL;DR: In this article, Fourier transform infrared (FTIR) spectroscopy was used to distinguish the cellular prion protein PrPC from its infectious analogue PrPSc, revealing a major conformational difference.
Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
S. Brahms,J.G. Brahms +1 more
TL;DR: By including all types of secondary structure and by enlarging substantially the spectral region, the method permits analysis of the conformation of a variety of proteins, such as nucleic acid-binding proteins, immunoglobulins and β-pleated sheet-rich proteins.
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