Journal
NATURE MEDICINE
Volume 10, Issue 10, Pages 1055-1063Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nm1113
Keywords
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Funding
- NIA NIH HHS [P01 AG14449, P01 AG17586, P01 AG11542, P30 AG10124, P01 AG14382, K08 AG20073-01, P01 AG09215] Funding Source: Medline
- NINDS NIH HHS [P01 NS044233] Funding Source: Medline
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A wide variety of neurodegenerative diseases are characterized by the accumulation of intracellular or extracellular protein aggregates. More recently, the genetic identification of mutations in familial counterparts to the sporadic disorders, leading to the development of in vitro and in vivo model systems, has provided insights into disease pathogenesis. The effect of many of these mutations is the abnormal processing of misfolded proteins that overwhelms the quality-control systems of the cell, resulting in the deposition of protein aggregates in the nucleus, cytosol and/or extracellular space. Further understanding of mechanisms regulating protein processing and aggregation, as well as of the toxic effects of misfolded neurodegenerative disease proteins, will facilitate development of rationally designed therapies to treat and prevent these disorders.
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