ATP synthase complex and the mitochondrial permeability transition pore: poles of attraction
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[1] Silvio C. E. Tosatto,et al. Ca2+ binding to F‐ATP synthase β subunit triggers the mitochondrial permeability transition , 2017, EMBO reports.
[2] L. Galluzzi,et al. Mitochondrial permeability transition involves dissociation of F1FO ATP synthase dimers and C‐ring conformation , 2017, EMBO reports.
[3] 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.
[4] J. Faraldo-Gómez,et al. Atomistic simulations indicate the c-subunit ring of the F1Fo ATP synthase is not the mitochondrial permeability transition pore , 2017, eLife.
[5] 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.
[6] John L Rubinstein,et al. Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM , 2015, bioRxiv.
[7] V. Giorgio,et al. Dimers of mitochondrial ATP synthase form the permeability transition pore , 2013, Proceedings of the National Academy of Sciences.
[8] L. Galluzzi,et al. Role of the c subunit of the FO ATP synthase in mitochondrial permeability transition , 2013, Cell cycle.
[9] A. Leslie,et al. Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1–ATPase from bovine heart mitochondria , 2012, Proceedings of the National Academy of Sciences.
[10] J. Rodríguez-Zavala,et al. The inhibitor protein (IF1) promotes dimerization of the mitochondrial F1F0-ATP synthase. , 2006, Biochemistry.