New insight in a new entity: the mitochondrial permeability transition pore arises from the Ca2+-activated F1FO-ATPases.

[1]  F. Trombetti,et al.  Kinetic properties of the mitochondrial F1FO-ATPase activity elicited by Ca2+ in replacement of Mg2. , 2017, Biochimie.

[2]  I. Fearnley,et al.  Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase , 2017, Proceedings of the National Academy of Sciences.

[3]  S. Nesci,et al.  Mitochondrial permeability transition, F1FO‐ATPase and calcium: an enigmatic triangle , 2017, EMBO reports.

[4]  Silvio C. E. Tosatto,et al.  Ca2+ binding to F‐ATP synthase β subunit triggers the mitochondrial permeability transition , 2017, EMBO reports.

[5]  L. Galluzzi,et al.  Mitochondrial permeability transition involves dissociation of F1FO ATP synthase dimers and C‐ring conformation , 2017, EMBO reports.

[6]  I. Fearnley,et al.  Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase , 2017, Proceedings of the National Academy of Sciences.

[7]  G. Lippe,et al.  The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology. , 2015, Physiological reviews.

[8]  W. Kühlbrandt,et al.  Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria , 2013, Proceedings of the National Academy of Sciences of the United States of America.

[9]  C. Bravo,et al.  Cross-Linking of the Endogenous Inhibitor Protein (IF1) with Rotor (γ,ε) and Stator (α) Subunits of the Mitochondrial ATP Synthase , 2002 .

[10]  C. Godinot,et al.  Docking the mitochondrial inhibitor protein IF1 to a membrane receptor different from the F1-ATPase beta subunit. , 1993, European journal of biochemistry.