Hugging tight in Huntington's
Mitochondrial fission-fusion and trafficking are altered in the fatal neurodegenerative disorder Huntington's disease. Huntingtin is now shown to function directly in these processes by binding the mitochondrial fission factor dynamin-related protein-1 (DRP1). Mutant huntingtin binds more tight...
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| Veröffentlicht in: | Nature medicine 2011-03, Vol.17 (3), p.245-246 |
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| creator | Johri, Ashu Chaturvedi, Rajnish K Beal, M Flint |
| description | Mitochondrial fission-fusion and trafficking are altered in the fatal neurodegenerative disorder Huntington's disease. Huntingtin is now shown to function directly in these processes by binding the mitochondrial fission factor dynamin-related protein-1 (DRP1). Mutant huntingtin binds more tightly to DRP1, leading to increased mitochondrial fission and neuronal death, highlighting DRP1 as a potential therapeutic target in Huntington's disease (
pages 377–382
). |
| doi_str_mv | 10.1038/nm0311-245 |
| format | Article |
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| subjects | 631/378/1689/1558 692/420 Binding sites Biomedical and Life Sciences Biomedicine Cancer Research Care and treatment GTP Phosphohydrolases - metabolism Humans Huntingtin Protein Huntington Disease - genetics Huntington Disease - metabolism Huntington Disease - physiopathology Huntington's chorea Huntingtons disease Infectious Diseases Metabolic Diseases Microtubule-Associated Proteins - metabolism Mitochondria Mitochondrial Proteins - metabolism Molecular Medicine Mutation Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Neurosciences news-and-views Nuclear Proteins - metabolism Nuclear Proteins - physiology Physiological aspects Protein Binding Proteins |
| title | Hugging tight in Huntington's |
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