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- W745996858 abstract "Neurodegenerative diseases involve a small set of proteins, called amyloids, which display exceptional conformational versatility. These proteins have no sequence homology but share remarkable properties, especially the capability to self-aggregate into highly ordered oligomers and fibrils with neurotoxic potential. In this chapter, we summarize the basic notions of protein structure that are indispensable to understand why and how these proteins can change their shape and form toxic aggregates. We analyze the molecular and thermodynamic mechanisms that control protein folding and plasticity in both water and membrane environments. We dissect the chaperone/antichaperone roles of lipid rafts in the generation of neurotoxic oligomers of amyloid proteins. We suggest that the sphingolipid-binding domain (SBD), which is structurally conserved in amyloid proteins, forms a common epitope recognized by a universal antioligomer antibody that blocks oligomer toxicity. We conclude that the SBD is a target of choice for a universal therapy against all neurodegenerative diseases." @default.
- W745996858 created "2016-06-24" @default.
- W745996858 creator A5047254221 @default.
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- W745996858 date "2015-01-01" @default.
- W745996858 modified "2023-09-27" @default.
- W745996858 title "Common Mechanisms in Neurodegenerative Diseases" @default.
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- W745996858 doi "https://doi.org/10.1016/b978-0-12-800111-0.00008-4" @default.
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