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10.4161/15384101.2014.949082 http://scihub22266oqcxt.onion/10.4161/15384101.2014.949082 C4612113!4612113 !25486353     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25486353 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Cell+Cycle 2014 ; 13 (17 ): 2666-70 Nephropedia Template TP {{tp|p=25486353 |t=2014. Novel insights into the mitochondrial permeability transition |pdf=|usr=}}{{25486353 }} gab.com Text Novel insights into the mitochondrial permeability transition JO: Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25486353 #FOAvip 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. Twit Text FOAVip Novel insights into the mitochondrial permeability transition ????Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25486353 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25486353 #FOAvip English Wikipedia <ref>{{Cite pmid|25486353 }}</ref> 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]Novel insights into the mitochondrial permeability transition (epmc).pdf DeepDyve Pubget Overpricing