title: Will preventing protein aggregates live up to its promise as prophylaxis against neurodegenerative diseases?
abstract: Protein aggregation and misfolding characterize most age-related neurodegenerative diseases including Alzheimer, Parkinson and Huntington diseases. Protein aggregation has generally been assumed to be responsible for neurodegeneration in these disorders due to association and genetics. However, protein aggregation may, in fact, be an attempt to protect neurons from the stress resulting from the disease etiology. In this review, we weigh the evidence of whether removal of amyloids, aggregates and neuronal inclusions represent a reasonable strategy for protecting neurons.
authors.affiliation: Institute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
authors.forename: Hyoung-gon
authors.initials: HG
authors.lastname: Lee
authors.forename: Robert B
authors.initials: RB
authors.lastname: Petersen
authors.forename: Xiongwei
authors.initials: X
authors.lastname: Zhu
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Honda
authors.forename: Gjumrakch
authors.initials: G
authors.lastname: Aliev
authors.forename: Mark A
authors.initials: MA
authors.lastname: Smith
authors.forename: George
authors.initials: G
authors.lastname: Perry
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D011232:Chemical Precipitation; D018890:Chemoprevention; D006801:Humans; D002479:Inclusion Bodies; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000517:prevention & control; D009474:Neurons / Q000378:metabolism*; D018384:Oxidative Stress; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D012307:Risk Factors
chemical_list: D000682:Amyloid; D011506:Proteins