
pmid: 17190592
Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion. Instead, they suggest that toxicity is solely due to interactions of Ataxin-1 with its normal binding partners.
Biochemistry, Genetics and Molecular Biology(all), Models, Neurological, Nuclear Proteins, Nerve Tissue Proteins, Neurodegenerative Diseases, Repressor Proteins, Mice, Ataxins, Mutation, Animals, Humans, Spinocerebellar Ataxias, Drosophila, Peptides, Ataxin-1
Biochemistry, Genetics and Molecular Biology(all), Models, Neurological, Nuclear Proteins, Nerve Tissue Proteins, Neurodegenerative Diseases, Repressor Proteins, Mice, Ataxins, Mutation, Animals, Humans, Spinocerebellar Ataxias, Drosophila, Peptides, Ataxin-1
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