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Many of the most common neurodegenerative diseases such as Alzheimer’s disease (AD), are characterized by aggregates of misfolded proteins that can occur intracellularly and extracellularly. In most cases, the accumulation of these misfolded proteins are predominant in dead cells. However, in some cases, these protein aggregates are absent in neurodegenerative cells. Due to this disparity, many studies believe that the protein aggregates are not toxic to cells since they do not contribute to neurodegeneration. By comparing the protein aggregates of AD, Parkinson’s disease (PD), Huntington disease (HD), and Transmissible spongiform encephalophaties (TSEs), we demonstrate that the protein aggregates of these diseases can indeed be toxic depending on the structure of the protein aggregates. As a result, we suggest that future studies should focus on targeting protein aggregates or understanding the mechanism behind their toxicity in order to develop better therapeutics against neurodegeneration.
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