Article
An Aβ42 variant that inhibits intra- and extracellular amyloid aggregation and enhances cell viability.
The Biochemical journal - 9 Oct 2018
Oren Ofek, Banerjee Victor, Taube Ran, Papo Niv
Abstract excerpt
Aggregation and accumulation of the 42-residue amyloid β peptide (Aβ42) in the extracellular matrix and within neuronal cells is considered a major cause of neuronal cell cytotoxicity and death in Alzheimer's disease (AD) patients. Therefore, molecules that bind to Aβ42 and prevent its aggregation are therapeutically promising as AD treatment. Here, we show that a non-self-aggregating Aβ42 variant carrying two...
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