Effects of oxidative and nitrative challenges on α-synuclein fibrillogenesis involve distinct mechanisms of protein modifications
EH Norris, BI Giasson, H Ischiropoulos… - Journal of Biological …, 2003 - ASBMB
Filamentous inclusions of α-synuclein protein are hallmarks of neurodegenerative diseases
collectively known as synucleinopathies. Previous studies have shown that exposure to
oxidative and nitrative species stabilizes α-synuclein filaments in vitro, and this stabilization
may be due to dityrosine cross-linking. To test this hypothesis, we mutated tyrosine residues
to phenylalanine and generated recombinant wild type and mutant α-synuclein proteins. α-
Synuclein proteins lacking some or all tyrosine residues form fibrils to the same extent as the …
collectively known as synucleinopathies. Previous studies have shown that exposure to
oxidative and nitrative species stabilizes α-synuclein filaments in vitro, and this stabilization
may be due to dityrosine cross-linking. To test this hypothesis, we mutated tyrosine residues
to phenylalanine and generated recombinant wild type and mutant α-synuclein proteins. α-
Synuclein proteins lacking some or all tyrosine residues form fibrils to the same extent as the …
