[HTML][HTML] Functional consequences of α-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation
R Hodara, EH Norris, BI Giasson… - Journal of Biological …, 2004 - ASBMB
Previous studies have shown the presence of nitrated α-synuclein (α-syn) in human Lewy
bodies and other α-syn inclusions. Herein, the effects of tyrosine nitration on α-syn fibril
formation, lipid binding, chaperone-like function, and proteolytic degradation were
systematically examined by employing chromatographically isolated nitrated monomeric,
dimeric, and oligomeric α-syn. Nitrated α-syn monomers and dimers but not oligomers
accelerated the rate of fibril formation of unmodified α-syn when present at low …
bodies and other α-syn inclusions. Herein, the effects of tyrosine nitration on α-syn fibril
formation, lipid binding, chaperone-like function, and proteolytic degradation were
systematically examined by employing chromatographically isolated nitrated monomeric,
dimeric, and oligomeric α-syn. Nitrated α-syn monomers and dimers but not oligomers
accelerated the rate of fibril formation of unmodified α-syn when present at low …