Quantification of Ataxin-3 and Ataxin-7 aggregates formed in vivo in Drosophila reveals a threshold of aggregated polyglutamine proteins associated with cellular toxicity - Vinatier, Gérald; Corsi, Jean-Marc; Mignotte, Bernard; Gaumer, Sébastien (Biochemical and biophysical research communications, 2015)
Keywords: Aging - genetics; Aging - metabolism; Aging - pathology; Animals; Animals, Genetically Modified; Ataxin-3 - chemistry; Ataxin-3 - genetics; Ataxin-3 - metabolism; Ataxin-7 - chemistry; Ataxin-7 - genetics; Ataxin-7 - metabolism; cell death; cytotoxicity; Disease Models, Animal; Drosophila; Drosophila melanogaster; Drosophila melanogaster - genetics; Drosophila melanogaster - metabolism; Female; Heredodegenerative Disorders, Nervous System - genetics; Heredodegenerative Disorders, Nervous System - metabolism; Heredodegenerative Disorders, Nervous System - pathology; Humans; Life Sciences; Male; Models, Neurological; Mutant Proteins - chemistry; Mutant Proteins - genetics; Mutant Proteins - metabolism; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Polyglutamine disease; Protein Aggregates; Protein Aggregation, Pathological - genetics; Protein Aggregation, Pathological - metabolism; proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Repressor Proteins - chemistry; Repressor Proteins - genetics; Repressor Proteins - metabolism; SCA3; SCA7; Solubility; Polyglutamine disease; SCA7; SCA3; Drosophila melanogaster; Protein aggregates