||P.6687 left column 2nd paragraph: "Unlike phosphorylation, truncations of α-synuclein correlate with enhanced aggregation in vitro and in vivo. C-terminal truncations are found in intracellular α-synuclein deposits (refs 672, 684-686) and they aggregate more readily in vitro (Table 2)(refs 52, 687-690). Indeed, removing C-terminal parts of the protein produces aggregation prone species with a decrease in net charge and an increase in hydrophobicity, as well as critical perturbations of autoinhibitory conformations that counteract aggregation of full-length α-synuclein (refs 676, 677). Aggregated α-synuclein isolated from post-mortem PD [Parkinson's disease] patients’ brains, exhibits a number of nonenzymatic and oxidative stress-associated modifications, such as tyrosine nitration, methionine oxidation and lipidation (ref 689). Many of these modifications were carefully investigated given their prominence in the disease (refs 607, 609, 691-695). Nitration of monomeric α-synuclein, for example, produces partially folded species that readily aggregate into off-pathway oligomers, inhibiting amyloid formation (Table 2)(refs 696, 697)." See notes beneath table.