Substantial evidence suggests that the aggregation of the presynaptic protein α-synuclein is
a key step in the etiology of Parkinson's disease (PD). Although the molecular mechanisms
underlying α-synuclein aggregation remain unknown, oxidative stress has been implicated
in the pathogenesis of PD. Here, we report the effects of tyrosine nitration on the propensity
of human recombinant α-synuclein to fibrillate in vitro. The properties of nitrated α-synuclein
were investigated using a variety of biophysical and biochemical techniques, which …