The Toxicity of Protein Aggregates in Several Neurodegenerative Diseases

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Ibraheem Alimi

Abstract




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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Author Biography

Ibraheem Alimi, Trent University

Ibraheem Alimi is a Managing Editor for JMRT as well as a Master’s of Science Candidate at Trent University within the Environmental and Life Sciences Graduate Program with a specialization in Cell Biology and Genetics.  Before coming to Trent, Ibraheem received his H.BSc degree from the University of Toronto with a specialization in Molecular Biology & Biotechnology.  Ibraheem is currently working as a member of the Saville Laboratory and Emery Laboratory and his research is focused on investigating the molecular mechanisms behind the formation of tumors in the corn smut disease.