Corruption and Spread of Pathogenic Proteins in Neurodegenerative Diseases |
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Authors: | Lary C Walker Harry LeVine III |
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Institution: | From the ‡Yerkes National Primate Research Center and Department of Neurology, Emory University, Atlanta, Georgia 30329 and ;the §Center on Aging, Center for Structural Biology, and Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536 |
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Abstract: | With advancing age, the brain becomes increasingly susceptible to neurodegenerative diseases, most of which are characterized by the misfolding and errant aggregation of certain proteins. The induction of aggregation involves a crystallization-like seeding mechanism by which a specific protein is structurally corrupted by its misfolded conformer. The latest research indicates that, once formed, proteopathic seeds can spread from one locale to another via cellular uptake, transport, and release. Impeding this process could represent a unified therapeutic strategy for slowing the progression of a wide range of currently intractable disorders. |
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Keywords: | Aging Alzheimer Disease Amyloid Amyotrophic Lateral Sclerosis (Lou Gehrig Disease) Huntington Disease Parkinson Disease Prions Protein Folding Proteopathy Seeding |
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