title: Prion-like spread of protein aggregates in neurodegeneration.
abstract: Protein misfolding is common to most neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. Recent work using animal models with intracellular α-synuclein and tau inclusions adds decisively to a growing body of evidence that misfolded protein aggregates can induce a self-perpetuating process that leads to amplification and spreading of pathological protein assemblies. When coupled with the progressive nature of neurodegeneration, recognition of such cell-to-cell aggregate spread suggests a unifying mechanism underlying the pathogenesis of these disorders.
authors.affiliation: Ludwig Institute for Cancer Research and Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
authors.forename: Magdalini
authors.initials: M
authors.lastname: Polymenidou
authors.forename: Don W
authors.initials: DW
authors.lastname: Cleveland
mesh_terms: D000818:Animals; D006801:Humans; D051379:Mice; D019636:Neurodegenerative Diseases / Q000209:etiology* / Q000503:physiopathology*; D016874:Neurofibrillary Tangles / Q000737:chemistry* / Q000473:pathology; D011328:Prions / Q000737:chemistry*; D057165:Proteostasis Deficiencies / Q000150:complications* / Q000503:physiopathology*; D051844:alpha-Synuclein / Q000737:chemistry*; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D011328:Prions; D051844:alpha-Synuclein; D016875:tau Proteins