Novel insights into the mitochondrial permeability transition |
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| Authors: | Massimo Bonora José Manuel Bravo-San Pedro Guido Kroemer |
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| Affiliation: | 1. Section of Pathology, Oncology and Experimental Biology;2. Laboratory for Technologies of Advanced Therapies (LTTA);3. Department of Morphology, Surgery and Experimental Medicine;4. University of Ferrara;5. Ferrara, Italy;6. Equipe 11 labelisée par la Ligue Nationale contre le cancer, Centre de Recherche des Cordeliers;7. Paris, France;8. INSERM, U1138;9. Gustave Roussy Comprehensive Cancer Center;10. Villejuif, France;11. Université Paris Descartes/Paris 5;12. Sorbonne Paris Cité;13. Metabolomics and Cell Biology platforms, Gustave Roussy Comprehensive Cancer Center;14. P?le de Biologie, H?pital Européen Georges Pompidou;15. AP-HP |
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| Abstract: | Alavian and colleagues recently provided further evidence in support of the notion that the c subunit of the mitochondrial F1FO ATP synthase constitutes the long-sought pore-forming unit of the supramolecular complex responsible for the so-called ‘mitochondrial permeability transition’ (MPT). Besides shedding new light on the molecular mechanisms that underlie the MPT, these findings corroborate the notion that several components of the cell death machinery, including cytochrome c and the F1FO ATP synthase, mediate critical metabolic activities. |
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| Keywords: | apoptosis BCL-XL cyclophilin D cyclosporin A necrosis permeability transition pore complex |
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