title: Corruption and spread of pathogenic proteins in neurodegenerative diseases.
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.
authors.affiliation: Yerkes National Primate Research Center and Department of Neurology, Emory University, Atlanta, Georgia 30329, USA. lary.walker@emory.edu
authors.forename: Lary C
authors.initials: LC
authors.lastname: Walker
authors.forename: Harry
authors.initials: H
authors.lastname: LeVine
mesh_terms: D000375:Aging; D058227:Amyloidogenic Proteins / Q000737:chemistry; D000818:Animals; D001921:Brain / Q000378:metabolism; D006624:Hippocampus / Q000473:pathology; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism; D020961:Lewy Body Disease / Q000378:metabolism; D051379:Mice; D008822:Mice, Transgenic; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D010300:Parkinson Disease / Q000378:metabolism; D011328:Prions / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D058227:Amyloidogenic Proteins; D011328:Prions