Neuropathology, Biochemistry, and Biophysics of α-synuclein Aggregation
Document Type
Article
Publication Date
2007
Digital Object Identifier (DOI)
https://doi.org/10.1111/j.1471-4159.2007.04764.x
Abstract
Aggregation of α-synuclein, an abundant and conserved pre-synaptic brain protein, is implicated as a critical factor in several neurodegenerative diseases. These diseases, known as synucleinopathies, include Parkinson’s disease, dementia with Lewy bodies (LBs), diffuse LB disease, the LB variant of Alzheimer’s disease, multiple system atrophy, and neurodegeneration with brain iron accumulation type I. Although the precise nature of in vivoα-synuclein function remains elusive, considerable knowledge has been accumulated about its structural properties and conformational behavior. α-Synuclein is a typical natively unfolded protein. It is characterized by the lack of rigid, well-defined, 3-D structure and possesses remarkable conformational plasticity. The structure of this protein depends dramatically on its environment and it accommodates a number of unrelated conformations. This paper provides an overview of the biochemistry, biophysics, and neuropathology of α-synuclein aggregation.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Neurochemistry, v. 103, issue 1, p. 17-37
Scholar Commons Citation
Uversky, Vladimir N., "Neuropathology, Biochemistry, and Biophysics of α-synuclein Aggregation" (2007). Molecular Medicine Faculty Publications. 782.
https://digitalcommons.usf.edu/mme_facpub/782
