However, the role of Hsp90 in regulating protein misfolding is not yet fully understood. The heat shock protein (Hsp) family, particularly Hsp70 and Hsp90, plays a major part in this process and it is well-known to regulate protein misfolding in a variety of diseases, including tau levels and toxicity in AD. They form an important line of defense against misfolded proteins and are part of the cellular quality control system. Chaperones and co-chaperones regulate protein folding and client maturation, but they also target misfolded or aggregated proteins for refolding or for degradation, mostly by the proteasome. Assembles of beta-amyloid (Aβ) peptide-either soluble (oligomers) or insoluble (plaques) and of tau protein, which form neurofibrillary tangles, are the major hallmarks of AD. The accumulation of misfolded proteins in the human brain is one of the critical features of many neurodegenerative diseases, including Alzheimer's disease (AD). 6Department of Anatomy and Cell Biology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, ON, Canada.5Department of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada.4Department of Pathology and Laboratory Medicine, University of Western Ontario, London, ON, Canada.3Department of Biochemistry, University of Western Ontario, London, ON, Canada.2Program in Neuroscience, University of Western Ontario, London, ON, Canada.1Molecular Medicine, Robarts Research Institute, University of Western Ontario, London, ON, Canada.Ostapchenko 1, Jose Marques-Lopes 1, Wing-Yiu Choy 3, Martin L. Lackie 1,2, Andrzej Maciejewski 1,3, Valeriy G.
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