期刊
ANNUAL REVIEW OF GENETICS, VOL 50
卷 50, 期 -, 页码 329-346出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-genet-120215-034943
关键词
A beta; Alzheimer's disease; amyloid; Parkinson's disease; prion; synuclein; tau
资金
- NCRR NIH HHS [P51 RR000165] Funding Source: Medline
- NIA NIH HHS [R21 AG040589, P50 AG025688] Funding Source: Medline
- NIH HHS [P51 OD011132] Funding Source: Medline
- NINDS NIH HHS [P30 NS055077] Funding Source: Medline
Most age-related neurodegenerative diseases are associated with the misfolding and aberrant accumulation of specific proteins in the nervous system. The proteins self-assemble and spread by a prion-like process of corruptive molecular templating, whereby abnormally folded proteins induce the misfolding and aggregation of like proteins into characteristic lesions. Despite the apparent simplicity of this process at the molecular level, diseases such as Alzheimer's, Parkinson's, Creutzfeldt-Jakob, and others display remarkable phenotypic heterogeneity, both clinically and pathologically. Evidence is growing that this variability is mediated, at least in part, by the acquisition of diverse molecular architectures by the misfolded proteins, variants referred to as proteopathic strains. The structural and functional diversity of the assemblies is influenced by genetic, epigenetic, and local contextual factors. Insights into proteopathic strains gleaned from the classical prion diseases can be profitably incorporated into research on other neurodegenerative diseases. Their potentially wide-ranging influence on disease phenotype also suggests that proteopathic strains should be considered in the design and interpretation of diagnostic and therapeutic approaches to these disorders.
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