Amino Acid Determinants of α-synuclein Aggregation: Putting Together Pieces of The Puzzle
Document Type
Article
Publication Date
2002
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(02)02883-1
Abstract
Parkinson's disease is the second most common neurodegenerative disease, and results from loss of dopaminergic neurons in the substantia nigra. The aggregation and fibrillation of α-synuclein in the form of intracellular proteinaceous aggregates (Lewy bodies and Lewy neurites) have been implicated as a causative factor in this disease, as well as in several other neurodegenerative disorders, including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, multiple system atrophy and Hallervorden–Spatz disease. Thus, the aggregated forms of α-synuclein play a crucial role in the pathogenesis of the synucleinopathies. However, the molecular mechanisms underlying α-synuclein aggregation into specific filamentous inclusions remained unknown until recently. Data on the aggregation and fibrillation properties of human α-, β- and γ-synucleins, mouse α-synuclein and familial Parkinson's disease mutants of human α-synuclein (A30P and A53T) are analyzed in order to shed light on the amino acid determinants of synuclein aggregation.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 522, issue 1-3, p. 9-13
Scholar Commons Citation
Uversky, Vladimir N. and Fink, Anthony L., "Amino Acid Determinants of α-synuclein Aggregation: Putting Together Pieces of The Puzzle" (2002). Molecular Medicine Faculty Publications. 694.
https://digitalcommons.usf.edu/mme_facpub/694
