Article
Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.
PloS one - 1 Jan 2009
Oztug Durer Zeynep A, Cohlberg Jeffrey A, Dinh Phong, Padua Shelby, Ehrenclou Krista, Downes Sean, Tan James K, Nakano Yoko, Bowman Christopher J, Hoskins Jessica L, Kwon Chuhee, Mason Andrew Z, Rodriguez Jorge A, Doucette Peter A, Shaw Bryan F, Valentine Joan Selverstone
Abstract excerpt
Mutations in the gene encoding Cu-Zn superoxide dismutase (SOD1) are one of the causes of familial amyotrophic lateral sclerosis (FALS). Fibrillar inclusions containing SOD1 and SOD1 inclusions that bind the amyloid-specific dye thioflavin S have been found in neurons of transgenic mice expressing mutant SOD1. Therefore, the formation of amyloid fibrils from human SOD1 was investigated. When agitated at acidic pH...
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