161,132 research outputs found

    Mitochondrial permeability transition, F<sub>1</sub><scp>F<sub>O</sub></scp>‐<scp>ATP</scp>ase and calcium: an enigmatic triangle

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    In this article, it was erroneously stated that the F1FO-ATPase was identified as forming the permeability transition pore (PTP) in 2015, citing a recent review on this topic [1]. In fact, the first work pointing to a role of the F-ATP synthase in PTP formation was published in 2013 by Bonora et al [2] and by Giorgio et al [3]. The author apologizes for this error

    Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel

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    The c subunits, which constitute the c‐ring apparatus of the F(1)F(O)‐ATPase, could be the main components of the mitochondrial permeability transition pore (mPTP). The well‐known modulator of the mPTP formation and opening is the cyclophilin D (CyPD), a peptidyl‐prolyl cis‐trans isomerase. On the loop, which connects the two hairpin α‐helix of c subunit, is present the unique proline residue (Pro (40)) that could be a biological target of CyPD. Indeed, the proline cis‐trans isomerization might provide the switch that interconverts the open/closed states of the pore by pulling out the c‐ring lipid plug
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