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The mitochondrial permeability transition: Recent progress and open questions

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Cyclophilin D, Somehow a Master Regulator of Mitochondrial Function

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ATP Synthase c-Subunit Leak Causes Aberrant Cellular Metabolism in Fragile X Syndrome

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Dopamine Oxidation Products as Mitochondrial Endotoxins, a Potential Molecular Mechanism for Preferential Neurodegeneration in Parkinson’s Disease

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The Mitochondrial Permeability Transition Pore and ATP Synthase

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The Unique Cysteine of F-ATP Synthase OSCP Subunit Participates in Modulation of the Permeability Transition Pore

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Mitochondrial Membrane Potential (ΔΨ) Fluctuations Associated with the Metabolic States of Mitochondria

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Mitochondrial F-ATP synthase as the permeability transition pore

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Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its F1 subcomplex

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Mitochondrial Ion Channels of the Inner Membrane and Their Regulation in Cell Death Signaling

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The mitochondrial chaperone TRAP1 regulates F-ATP synthase channel formation

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Electrophysiological properties of the mitochondrial permeability transition pores: Channel diversity and disease implication

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Zinc and calcium alter the relationship between mitochondrial respiration, ROS and membrane potential in rainbow trout (Oncorhynchus mykiss) liver mitochondria

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The Haves and Have-Nots: The Mitochondrial Permeability Transition Pore across Species

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Sulphoraphane Improves Neuronal Mitochondrial Function in Brain Tissue in Acute Carbon Monoxide Poisoning Rats

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Channel formation by F-ATP synthase and the permeability transition pore: an update

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The Mitochondrial Permeability Transition Pore

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Adenine nucleotide translocator and ATP synthase cooperate in mediating the mitochondrial permeability transition

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Cryo-EM structure of the brine shrimp mitochondrial ATP synthase suggests an inactivation mechanism for the ATP synthase leak channel

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Comprehensive analysis of regulated cell death pathways: intrinsic disorder, protein–protein interactions, and cross-pathway communication

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Human F-ATP synthase as a drug target

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Lithocholic acid induces two different calcium-dependent inner membrane permeability systems in liver mitochondria

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The Mitochondrial Permeability Transition Pore: Past, Present, and Future

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The Mitochondrial Permeability Transition Pore: Molecular Structure and Function in Health and Disease

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Bedaquiline inhibits the ATP synthase leak channel and prevents glutamate-induced neuronal death

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ATP synthase: Structure, function, and channel formation

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Mitochondrial Membrane Potential (ΔΨ) Fluctuations Associated with the Metabolic States of Mitochondria

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Induction of the Ca2+-Dependent Permeability Transition in Liver Mitochondria by α,ω-Hexadecanedioic Acid is Blocked by Inorganic Phosphate in the Presence of Cyclosporin A

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Structure and function of the intermembrane space domain of mammalian F o F 1 ATP synthasePreprint

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19th European Bioenergetics Conference—Preface

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ЛИТОХОЛЕВАЯ КИСЛОТА ИНДУЦИРУЕТ ДВЕ РАЗЛИЧНЫЕ КАЛЬЦИЙ-ЗАВИСИМЫЕ СИСТЕМЫ ПРОНИЦАЕМОСТИ ВНУТРЕННЕЙ МЕМБРАНЫ В МИТОХОНДРИЯХ ПЕЧЕНИ, "Биологические мембраны: Журнал мембранной и клеточной биологии"

Dubinin, M. V., Khoroshavina, E. I., & Самарцев, В. Н. (2017) · Биологические мембраны Журнал мембранной и клеточной биологии · doi:10.7868/s0233475517030045

A Comparative Study of the Effects of Palmitic Acid and ω-Hydroxypalmitic Acid as Inducers of Ca2+-Dependent Permeabilization of Liver Mitochondria and Lecithin Liposomes

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Rejuvenating the Mitochondrial Permeability Transition

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Développement de nouvelles approches thérapeutiques en virologie et hépatologie : Small-Molecule Cyclophilin Inhibitors (SMCypI)

Ruiz, I. (2019) · doi:10.70675/fdbace6az69e8z4704za369z9e1f198d9abc

Étude de l'effet de nouveaux ligands de la cyclophiline D sur le pore de transition de perméabilité mitochondrial et de leur effet protecteur

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ATP synthase subunits e and g are essential for Ca2+ homeostasis and development in Drosophila melanogaster independent of oxidative phosphorylation

Frigo, E., Santalla, M., Brischigliaro, M., Nata, F. B., Tommasin, L., Rossini, M., Komarov, D., Ferro, S., Pendin, D., Marin, O., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01869-5

Mitochondrial F-ATP synthase as the permeability transition pore

Gerle, C. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105081 · Cited by 54 · see citing works

Why F-ATP Synthase Remains a Strong Candidate as the Mitochondrial Permeability Transition Pore

Bernardi, P. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01543 · Cited by 46 · see citing works

Channel formation by F-ATP synthase and the permeability transition pore: an update

Bernardi, P., & Lippe, G. (2017) · Current Opinion in Physiology · doi:10.1016/j.cophys.2017.12.006 · Cited by 13 · see citing works

What Makes You Can Also Break You, Part II: Mitochondrial Permeability Transition Pore Formation by Dimers of the F1FO ATP-Synthase?

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ATP synthase complex and the mitochondrial permeability transition pore: poles of attraction

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