Pub. Date : 2010 Feb
PMID : 20104018
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | In this study we explore the role for autophagy in the clearance of an N-terminal caspase-7-generated fragment of ataxin-7, a protein with a pathogenic polyglutamine (polyQ) expansion in the neurodegenerative disease spinocerebellar ataxia 7 (SCA7). | polyglutamine | ataxin 7 | Mus musculus |
2 | In this study we explore the role for autophagy in the clearance of an N-terminal caspase-7-generated fragment of ataxin-7, a protein with a pathogenic polyglutamine (polyQ) expansion in the neurodegenerative disease spinocerebellar ataxia 7 (SCA7). | polyglutamine | ataxin 7 | Mus musculus |
3 | Using both cellular and transgenic mouse models of SCA7 we show that the stability of wild-type ataxin-7 is modified by macroautophagy, but not by proteasomal, inhibition, whereas both autophagy and proteasomal degradation have little effect on polyQ-expanded ataxin-7. | polyglutamine | ataxin 7 | Mus musculus |
4 | We also create a post-translational modification-deficient ataxin-7 mutant that has increased protein turnover of both wild-type and polyQ-expanded ataxin-7, mediated through the autophagy pathway. | polyglutamine | ataxin 7 | Mus musculus |
5 | We also create a post-translational modification-deficient ataxin-7 mutant that has increased protein turnover of both wild-type and polyQ-expanded ataxin-7, mediated through the autophagy pathway. | polyglutamine | ataxin 7 | Mus musculus |