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10.4161/15384101.2014.949082

http://scihub22266oqcxt.onion/10.4161/15384101.2014.949082
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C4612113!4612113 !25486353
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suck abstract from ncbi

pmid25486353
      Cell+Cycle 2014 ; 13 (17 ): 2666-70
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  • Novel insights into the mitochondrial permeability transition #MMPMID25486353
  • Bonora M ; Bravo-San Pedro JM ; Kroemer G ; Galluzzi L ; Pinton P
  • Cell Cycle 2014[]; 13 (17 ): 2666-70 PMID25486353 show ga
  • 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.
  • |Animals [MESH]
  • |Humans [MESH]
  • |Mitochondrial Membrane Transport Proteins/*metabolism [MESH]
  • |Mitochondrial Permeability Transition Pore [MESH]
  • |Mitochondrial Proton-Translocating ATPases/metabolism [MESH]


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