Abstract
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.
Keywords
IntracellularProtein aggregationExtracellularProtein foldingCytosolDiseaseNeuroscienceBiologyNeurodegenerationPathogenesisCell biologyMedicineImmunologyBiochemistryEnzymePathology
MeSH Terms
Alzheimer DiseaseAmyloid beta-PeptidesAmyotrophic Lateral SclerosisCreutzfeldt-Jakob SyndromeHistory20th CenturyHistory21st CenturyHumansLewy BodiesModelsBiologicalNerve Tissue ProteinsNeurodegenerative DiseasesPeptidesPrionsProtein FoldingSuperoxide DismutaseSynucleins
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Publication Info
- Year
- 2004
- Type
- review
- Volume
- 10
- Issue
- 10
- Pages
- 1055-1063
- Citations
- 692
- Access
- Closed
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Cite This
Mark S. Forman,
John Q. Trojanowski,
Virginia M.‐Y. Lee
(2004).
Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs.
Nature Medicine
, 10
(10)
, 1055-1063.
https://doi.org/10.1038/nm1113
Identifiers
- DOI
- 10.1038/nm1113
- PMID
- 15459709