α-synuclein Misfolding and Parkinson's Disease
α-synuclein, Parkinson's Disease, Neurodegeneration, Aggregation, Intrinsically Disordered Protein, Metal-exposure
Digital Object Identifier (DOI)
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.
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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.