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Many human movement disorders are caused by protein misfolding and aggregation in neurons and glia. Parkinson's disease and multiple system atrophy are characterized by accumulation of misfolded alpha-synuclein, whereas misfolded MAP-tau accumulates in progressive supranuclear palsy and corticobasal degeneration. In addition, primary torsion dystonia is caused by loss of function of torsin, an endoplasmic reticulum chaperone. We have generated novel zebrafish models allowing us to study the pathogenesis of these diseases and to isolate chemical modifiers as a first step towards drug discovery. We also have a research program evaluating gene therapy approaches in these diseases.