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Title[redir]:
Dimers of mitochondrial ATP syntha ... | Article | H1 Connect
Description:
Here we define the molecular nature of the mitochondrial permeability transition pore (PTP), a key effector of cell death. The PTP is regulated by matrix c

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Keywords {🔍}

mitochondrial, permeability, transition, mptp, latest, recommendation, atp, pore, synthase, finding, formation, drug, dimers, interesting, discovery, faculty, giorgio, confirmation, jun, molecular, complex, channel, membrane, role, design, cell, biology, death, physiology, jan, feb, eduardo, rial, apr, show, components, demonstrated, forms, mitochondria, cyclophilind, sensitivity, subunit, demonstrate, essential, views, development, dysfunction, macromolecular, assemblies, machines,

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mitochondrial-dependent cell death recombinant adp/atp carrier permeability transition pore mitochondrial permeability transition cell death molecular components molecular structure interesting paper reporting mitochondrial megachannel resides adp/atp translocator atp synthase monomer fo atp synthase adjacent f0 subunits explore unresolved issues neurospora crassa resembles atpase c-subunit mitochondria matrix cyclophilin 2007 controversial refutation faculty opinions atp synthase mitochondrial protection interesting development dysfunction due voltage threshold h1 company latest recommendation 2016 latest recommendation 13 latest recommendation atp synthesis mitochondria devoid finding evaluations finding loss finding properties archived dimers finding role doctors search national academy united states dual function defined regulator authors confirmed previous data {3} lateral stalk rna interference expression augments lipid bilayers current typical membrane interface results provide pathophysiological conditions

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ScholarlyArticle:
      context:https://schema.org
      headline:Dimers of mitochondrial ATP synthase form the permeability transition pore.
      abstract:Here we define the molecular nature of the mitochondrial permeability transition pore (PTP), a key effector of cell death. The PTP is regulated by matrix cyclophilin D (CyPD), which also binds the lateral stalk of the FOF1 ATP synthase. We show that CyPD binds the oligomycin sensitivity-conferring protein subunit of the enzyme at the same site as the ATP synthase inhibitor benzodiazepine 423 (Bz-423), that Bz-423 sensitizes the PTP to Ca(2+) like CyPD itself, and that decreasing oligomycin sensitivity-conferring protein expression by RNAi increases the sensitivity of the PTP to Ca(2+). Purified dimers of the ATP synthase, which did not contain voltage-dependent anion channel or adenine nucleotide translocator, were reconstituted into lipid bilayers. In the presence of Ca(2+), addition of Bz-423 triggered opening of a channel with currents that were typical of the mitochondrial megachannel, which is the PTP electrophysiological equivalent. Channel openings were inhibited by the ATP synthase inhibitor AMP-PNP (γ-imino ATP, a nonhydrolyzable ATP analog) and Mg(2+)/ADP. These results indicate that the PTP forms from dimers of the ATP synthase.
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WebPage:
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