Article
Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice.
The Journal of biological chemistry - 3 Nov 2006
Basso Manuela, Massignan Tania, Samengo Giuseppina, Cheroni Cristina, De Biasi Silvia, Salmona Mario, Bendotti Caterina, Bonetto Valentina
Abstract excerpt
Mutations in the Cu,Zn-superoxide dismutase (SOD1) gene cause a familial form of amyotrophic lateral sclerosis (ALS) through an unknown gain-of-function mechanism. Mutant SOD1 aggregation may be the toxic property. In fact, proteinaceous inclusions rich in mutant SOD1 have been found in tissues from the familial form of ALS patients and in mutant SOD1 animals, before disease onset. However, very little is known...
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