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10.3390/ijms15057513 http://scihub22266oqcxt.onion/10.3390/ijms15057513 C4057687!4057687 !24786291     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24786291 &cmd=llinks): Failed to open stream: HTTP request failed! 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The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology |pdf=|usr=}}{{24786291 }} gab.com Text The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=24786291 #FOAvip The oligomycin-sensitivity conferring protein (OSCP) of the mitochondrial F(O)F1 ATP synthase has long been recognized to be essential for the coupling of proton transport to ATP synthesis. Located on top of the catalytic F1 sector, it makes stable contacts with both F1 and the peripheral stalk, ensuring the structural and functional coupling between F(O) and F1, which is disrupted by the antibiotic, oligomycin. Recent data have established that OSCP is the binding target of cyclophilin (CyP) D, a well-characterized inducer of the mitochondrial permeability transition pore (PTP), whose opening can precipitate cell death. CyPD binding affects ATP synthase activity, and most importantly, it decreases the threshold matrix CaČ? required for PTP opening, in striking analogy with benzodiazepine 423, an apoptosis-inducing agent that also binds OSCP. These findings are consistent with the demonstration that dimers of ATP synthase generate CaČ?-dependent currents with features indistinguishable from those of the PTP and suggest that ATP synthase is directly involved in PTP formation, although the underlying mechanism remains to be established. In this scenario, OSCP appears to play a fundamental role, sensing the signal(s) that switches the enzyme of life in a channel able to precipitate cell death. Twit Text FOAVip The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=24786291 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24786291 #FOAvip English Wikipedia <ref>{{Cite pmid|24786291 }}</ref> The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology #MMPMID24786291 Antoniel M ; Giorgio V ; Fogolari F ; Glick GD ; Bernardi P ; Lippe G Int J Mol Sci 2014[Apr]; 15 (5 ): 7513-36 PMID24786291 show ga The oligomycin-sensitivity conferring protein (OSCP) of the mitochondrial F(O)F1 ATP synthase has long been recognized to be essential for the coupling of proton transport to ATP synthesis. Located on top of the catalytic F1 sector, it makes stable contacts with both F1 and the peripheral stalk, ensuring the structural and functional coupling between F(O) and F1, which is disrupted by the antibiotic, oligomycin. Recent data have established that OSCP is the binding target of cyclophilin (CyP) D, a well-characterized inducer of the mitochondrial permeability transition pore (PTP), whose opening can precipitate cell death. CyPD binding affects ATP synthase activity, and most importantly, it decreases the threshold matrix CaČ? required for PTP opening, in striking analogy with benzodiazepine 423, an apoptosis-inducing agent that also binds OSCP. These findings are consistent with the demonstration that dimers of ATP synthase generate CaČ?-dependent currents with features indistinguishable from those of the PTP and suggest that ATP synthase is directly involved in PTP formation, although the underlying mechanism remains to be established. In this scenario, OSCP appears to play a fundamental role, sensing the signal(s) that switches the enzyme of life in a channel able to precipitate cell death. |Adenosine Triphosphatases/analysis/*metabolism [MESH] |Animals [MESH] |Carrier Proteins/analysis/*metabolism [MESH] |Cyclophilins/metabolism [MESH] |Humans [MESH] |Membrane Proteins/analysis/*metabolism [MESH] |Mitochondria/*metabolism/pathology [MESH] |Mitochondrial Membrane Transport Proteins/chemistry/metabolism [MESH] |Mitochondrial Permeability Transition Pore [MESH] |Mitochondrial Proton-Translocating ATPases/analysis/*metabolism [MESH] |Models, Molecular [MESH] |Peptidyl-Prolyl Isomerase F [MESH] |Protein Conformation [MESH]The oligomycin-sensitivity conferring protein of mitochondrial ATP syn(epmc).pdf DeepDyve Pubget Overpricing