Journal
NEURON
Volume 79, Issue 6, Pages 1044-1066Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2013.09.004
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Funding
- John and Helen Cahill Family Endowed Chair in Parkinson's Disease Research
- NIH
- Giannini Foundation
- NIH [NS062715]
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Human genetics has indicated a causal role for the protein alpha-synuclein in the pathogenesis of familial Parkinson's disease (PD), and the aggregation of synuclein in essentially all patients with PD suggests a central role for this protein in the sporadic disorder. Indeed, the accumulation of misfolded alpha-synuclein now defines multiple forms of neural degeneration. Like many of the proteins that accumulate in other neurodegenerative disorders, however, the normal function of synuclein remains poorly understood. In this article, we review the role of synuclein at the nerve terminal and in membrane remodeling. We also consider the prion-like propagation of misfolded synuclein as a mechanism for the spread of degeneration through the neuraxis.
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