α-synuclein Misfolding and Parkinson's Disease
Document Type
Article
Publication Date
2012
Keywords
α-synuclein, Parkinson's Disease, Neurodegeneration, Aggregation, Intrinsically Disordered Protein, Metal-exposure
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.bbadis.2011.10.002
Abstract
Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has been identified as the major component of Lewy bodies and Lewy neurites, the characteristic proteinaceous deposits that are the hallmarks of PD. α-Synuclein is a typical intrinsically disordered protein, but can adopt a number of different conformational states depending on conditions and cofactors. These include the helical membrane-bound form, a partially-folded state that is a key intermediate in aggregation and fibrillation, various oligomeric species, and fibrillar and amorphous aggregates. The molecular basis of PD appears to be tightly coupled to the aggregation of α-synuclein and the factors that affect its conformation. This review examines the different aggregation states of α-synuclein, the molecular mechanism of its aggregation, and the influence of environmental and genetic factors on this process.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, v. 1822, issue 2, p. 261-285
Scholar Commons Citation
Breydo, Leonid; Wu, Jessica W.; and Uversky, Vladimir N., "α-synuclein Misfolding and Parkinson's Disease" (2012). Molecular Medicine Faculty Publications. 492.
https://digitalcommons.usf.edu/mme_facpub/492
