Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference29 articles.
1. Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
2. Evidence for both nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington'sdisease in cell culture and in transgenic mice expressing mutant huntingtin
3. Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions
4. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
5. Caspase Cleavage of Gene Products Associated with Triplet Expansion Disorders Generates Truncated Fragments Containing the Polyglutamine Tract
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2. Insulin-Degrading Enzyme Efficiently Degrades polyQ Peptides but not Expanded polyQ Huntingtin Fragments;Journal of Huntington's Disease;2024-07-02
3. Progressive degeneration in a new Drosophila model of spinocerebellar ataxia type 7;Scientific Reports;2024-06-21
4. Pathobiology of the autophagy-lysosomal pathway in the Huntington’s disease brain;2024-05-30
5. mTOR inhibition in Q175 Huntington’s disease model mice facilitates neuronal autophagy and mutant huntingtin clearance;2024-05-30
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