Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition

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Cytochrome C -Mediated Apoptosis

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The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore

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Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria

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Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart

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Protection by Cyclosporin A of Ischemia/Reperfusion-Induced Damage in Isolated Rat Hearts

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The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents

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Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency

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A distinct sequence in the adenine nucleotide translocase from Artemia franciscana embryos is associated with insensitivity to bongkrekate and atypical effects of adenine nucleotides on Ca2+ uptake and sequestration

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Reprint of “The mitochondrial permeability transition pore and its adaptive responses in tumor cells”

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New Insights into the Role of Ubiquitin Networks in the Regulation of Antiapoptosis Pathways

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Cyclophilin D ablation is associated with increased end-ischemic mitochondrial hexokinase activity

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Reactive Oxygen Species: Friends and Foes of Signal Transduction

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Sphingosine impairs mitochondrial function by opening permeability transition pore

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Cyclophilin D Regulates the Nuclear Translocation of AIF, Cardiac Endothelial Cell Necroptosis and Murine Cardiac Transplant Injury

Qamar, A., Zhao, J., Xu, L., McLeod, P., Huang, X., Jiang, J., Liu, W., Haig, A. R., & Zhang, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011038 · Cited by 14

N-terminal cleavage of cyclophilin D boosts its ability to bind F-ATP synthase

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Cyclophilin D knockout protects the mouse kidney against cyclosporin A-induced oxidative stress

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Non-conventional mitochondrial permeability transition: Its regulation by mitochondrial dynamics

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New Therapies for Acute Myocardial Infarction: Current State of Research and Future Promise

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Inhibition of mitochondrial membrane bound-glutathione transferase by mitochondrial permeability transition inhibitors including cyclosporin A

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Gene expression profiling of the left ventricles in a rat model of intrinsic aerobic running capacity

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Deletion of the Mitochondrial Matrix Protein CyclophilinD Prevents Parvalbumin Interneuron Dysfunctionand Cognitive Deficits in a Mouse Model of NMDA Hypofunction

Phensy, A. J., Lindquist, K. L., Lindquist, K. A., Bairuty, D., Gauba, E., Guo, L., Tian, J., Du, H., & Kroener, S. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0880-20.2020 · Cited by 13

Ethylmalonic Acid Induces Permeability Transition in Isolated Brain Mitochondria

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Two Critical Factors Affecting the Release of Mitochondrial Cytochrome c as Revealed by Studies Using N,N′-Dicyclohexylcarbodiimide as an Atypical Inducer of Permeability Transition

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Cyclophilin D regulates lifespan and protein expression of aging markers in the brain of mice

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Structurally diverse peroxisome proliferator‐activated receptor agonists induce apoptosis in human uro‐epithelial cells by a receptor‐independent mechanism involving store‐operated calcium channels

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Release of intracellular calcium primes chronic myeloid leukaemia cells for tyrosine kinase inhibitor-induced apoptosis

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Role of the mitochondrial protein cyclophilin D in skin wound healing and collagen secretion

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

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Not all mitochondrial carrier proteins support permeability transition pore formation: no involvement of uncoupling protein 1

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6.4 Mitochondrial Permeability Transition in the CNS—Composition, Regulation, and Pathophysiological Relevance

Wieloch, T. W., Mattiasson, G., Hansson, M. J., & Elmér, E. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_25 · Cited by 11

Mitochondrial Permeability Transition

Brustovetsky, N. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch1 · Cited by 11

ROMO1 overexpression protects the mitochondrial cysteinome from oxidations in aging

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Nitric oxide scavenging modulates mitochondrial dysfunction induced by hypoxia/reoxygenation

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Cyclophilin inhibitor NIM811 ameliorates experimental allergic encephalomyelitis

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Two Metabolic Fuels, Glucose and Lactate, Differentially Modulate Exocytotic Glutamate Release from Cultured Astrocytes

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Proximal Events in 7,12-Dimethylbenz[a]anthracene-Induced, Stromal Cell-Dependent Bone Marrow B Cell Apoptosis: Stromal Cell–B Cell Communication and Apoptosis Signaling

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Induction of unspecific permeabilization of mitochondrial membrane and its role in cell death

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Mitochondrial Ion Channels

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Sevoflurane Induces a Cyclophilin D-Dependent Decrease of Neural Progenitor Cells Migration

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The Intrinsic Pathway of Apoptosis

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Extracellular ADP prevents neuronal apoptosis via activation of cell antioxidant enzymes and protection of mitochondrial ANT-1

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Cyclophilin D regulates necrosis, but not apoptosis, of murine eosinophils

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The novel cyclophilin-D-interacting protein FASTKD1 protects cells against oxidative stress-induced cell death

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p53 Is Potentially Regulated by Cyclophilin D in the Triple-Proline Loop of the DNA Binding Domain

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Hypoxic preconditioning-induced mitochondrial protection is not disrupted in a cell model of mtDNA T8993G mutation-induced F1F0-ATP synthase defect: the role of mitochondrial permeability transition

Huang, W., Jou, M., & Peng, T. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.019 · Cited by 8

Bisindolylpyrrole triggers transient mitochondrial permeability transitions to cause apoptosis in a VDAC1/2 and cyclophilin D-dependent manner via the ANT-associated pore

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Индукция неспецифической проницаемости митохондриальной мембраны и ее роль в гибели клеток

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Elevations in the Mitochondrial Matrix Protein Cyclophilin D Correlate With Reduced Parvalbumin Expression in the Prefrontal Cortex of Patients With Schizophrenia

O'Brien, J. T., Jalilvand, S. P., Suji, N. A., Jupelly, R. K., Phensy, A. J., Mwirigi, J. M., Elahi, H., Price, T. J., & Kroener, S. (2024) · Schizophrenia Bulletin · doi:10.1093/schbul/sbae016 · Cited by 7

Differential Ca2+ handling by isolated synaptic and non-synaptic mitochondria: roles of Ca2+ buffering and efflux

Mishra, J., Bevers, K., Li, K., Zare, A., Heisner, J. S., Tong, A., Kwok, W., Stowe, D. F., & Camara, A. K. S. (2025) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2025.1562065 · Cited by 7

Application of locally responsive design of biomaterials based on microenvironmental changes in myocardial infarction

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Endogenous Complement 1q Binding Protein (C1qbp) Regulates Mitochondrial Permeability Transition and Post-Myocardial Infarction Remodeling and Dysfunction

Gutiérrez-Aguilar, M., Klutho, P. J., Aguayo-Ortiz, R., Song, L., & Baines, C. P. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.08.005 · Cited by 6

Ciclosporin does not attenuate intracranial hypertension in rats with acute hyperammonaemia

Larsen, R. H. (2013) · World Journal of Hepatology · doi:10.4254/wjh.v5.i9.513 · Cited by 7

The mitochondrial unselective channel in Saccharomyces cerevisiae

Gutiérrez‐Aguilar, M., & Uribe‐Carvajal, S. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.04.002 · Cited by 7

High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules

Valasani, K. R., Carlson, E. A., Battaile, K. P., Bisson, A., Wang, C., Lovell, S., & Yan, S. S. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14009480 · Cited by 7

Assessing the molecular basis for rat-selective induction of the mitochondrial permeability transition by norbormide

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Ciclosporin to Protect Renal function In Cardiac Surgery (CiPRICS): a study protocol for a double-blind, randomised, placebo-controlled, proof-of-concept study

Ederoth, P., Grins, E., Dardashti, A., Brondén, B., Metzsch, C., Erdling, A., Nozohoor, S., Mokhtari, A., Hansson, M. J., Elmér, E., et al. (2016) · BMJ Open · doi:10.1136/bmjopen-2016-012299 · Cited by 7

Modelling the molecular mechanism of protein–protein interactions and their inhibition: CypD–p53 case study

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Disrupting cancer cell function by targeting mitochondria

Yan, S. S. (2014) · Integrative Cancer Science and Therapeutics · doi:10.15761/icst.1000105 · Cited by 7

Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca2+-Dependent Formation of Large Channels

Nikiforova, A. B., Baburina, Y. L., Borisova, M. P., Surin, A. K., Kharechkina, E. S., Krestinina, O. V., Suvorina, M. Y., Kruglova, S. A., & Kruglov, A. G. (2023) · Cells · doi:10.3390/cells12192414 · Cited by 6

Unveiling OSCP as the potential therapeutic target for mitochondrial dysfunction-related diseases

Zhang, M., Luo, X., Zhang, B., Luo, D., Huang, L.-Z., & Long, Q. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122293 · Cited by 7

The role and mechanism of VDAC1 in type 2 diabetes: An underestimated target of environmental pollutants

Ma, Y., Sun, X., & Yao, X. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101929 · Cited by 6

Mitochondrial permeability transition mediated by MTCH2 and F‐ ATP synthase contributes to ferroptosis defense

Guo, L. (2024) · FEBS Letters · doi:10.1002/1873-3468.15008 · Cited by 6

Pharmacological Targeting of the Mitochondrial Permeability Transition Pore for Cardioprotection

Silva, F. S. G., Costa, C. F., Marques, R., Oliveira, P. J., & Pereira, G. C. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_20 · Cited by 7

Infarct Size With Incremental Global Myocardial Ischemia Times: Cyclosporine A in Donation After Circulatory Death Rat Hearts

Quader, M. A., Akande, O., Cholyway, R. M., Lesnefsky, E. J., Toldo, S. A., & Chen, Q. (2023) · Transplantation Proceedings · doi:10.1016/j.transproceed.2023.03.088 · Cited by 6

Cyclophilin‐D is dispensable for atrophy and mitochondrial apoptotic signalling in denervated muscle

Daussin, F., Godin, R., Ascah, A., Deschênes, S., & Burelle, Y. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.202036 · Cited by 6

Reduced capacity of Ca2+ retention in liver as compared to kidney mitochondria. ADP requirement

Zazueta, C., Garcı́a, N., Abundis, E. M., Pavón, N., Hernández‐Esquivel, L., & Chávez, E. (2010) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-010-9300-0 · Cited by 6

Mitochondrial uncoupling protein-2 in glutamate neurotoxicity

Takarada, T., Fukumori, R., & Yoneda, Y. (2013) · Folia Pharmacologica Japonica · doi:10.1254/fpj.142.13 · Cited by 6

Effects of ubiquinone derivatives on the mitochondrial unselective channel of Saccharomyces cerevisiae

Gutiérrez‐Aguilar, M., López-Carbajal, H. M., Uribe‐Alvarez, C., Espinoza‐Simón, E., Rosas‐Lemus, M., Chiquete‐Félix, N., & Uribe‐Carvajal, S. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9595-3 · Cited by 6

Docosahexaenoic acid and butyrate synergistically induce colonocyte apoptosis by enhancing mitochondrial calcium accumulation

Kolar, S. S. N., Barhoumi, R., Callaway, E. S., Lupton, J. R., & Chapkin, R. S. (2007) · The FASEB Journal · doi:10.1096/fasebj.21.5.a158 · Cited by 6

Deficient Sarcolemma Repair in ALS: A Novel Mechanism with Therapeutic Potential

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Disturbance of mitochondrial functions caused by N-acetylglutamate and N-acetylmethionine in brain of adolescent rats: Potential relevance in aminoacylase 1 deficiency

Bortoluzzi, V. T., Ribeiro, R. T., Zemniaçak, Â. B., Cunha, S. D. A., Sass, J. O., Castilho, R. F., Amaral, A. U., & Wajner, M. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105631 · Cited by 5

Twist2 knockdown alleviates renal ischemia–reperfusion injury by maintaining mitochondrial function and enhancing mitophagy through Bnip3

Zhang, L., Ye, J., & Qiu, C. (2025) · Human Cell · doi:10.1007/s13577-025-01177-z · Cited by 5

Mitochondrial Dysfunction on the Toxic Effects of Anticancer Agents— From Lab Bench to Bedside

Ribeiro, M. P. C., Santos, A. E. C. E., & Custódio, J. B. A. (2015) · InTech eBooks · doi:10.5772/59488 · Cited by 7

La mitochondrie : une cible incontournable de la cardioprotection du myocarde ischémique

Argaud, L., Ovize, M., & Robert, D. (2006) · Réanimation · doi:10.1016/j.reaurg.2005.12.019 · Cited by 5

Trypanosoma cruzi infection in Cyclophilin D deficient mice

Milduberger, N., Bustos, P. L., González, C., Perrone, A. E., Postan, M., & Búa, J. (2020) · Experimental Parasitology · doi:10.1016/j.exppara.2020.108044 · Cited by 5

Cyclophilin D Regulates Oxidative Stress and Apoptosis via Mitochondrial Permeability Transition Pore in Acute Acalculous Cholecystitis

Hong, K., Yang, Q., Liu, G., Qiu, H., & Yu, B. (2022) · Current Molecular Medicine · doi:10.2174/1566524023666220908112922 · Cited by 5

The spatial and temporal relationship between oxidative stress and neuronal degeneration in 3-nitropropionic acid model

Delorme, T., Najafi, M., & Nasr, P. (2012) · World Journal of Neuroscience · doi:10.4236/wjns.2012.24036 · Cited by 5

The Impact of Astrocyte Mitochondrial Metabolism on Neuroprotection During Aging

Watts, L. T., & Lechleiter, J. D. (2008) · Springer eBooks · doi:10.1007/978-0-387-79492-1_23 · Cited by 5

Concussive Head Trauma Deranges Axon Initial Segment Function in Axotomized and Intact Layer 5 Pyramidal Neurons

Harris, A. C., Sun, J., & Jacobs, K. M. (2023) · Journal of Neurotrauma · doi:10.1089/neu.2022.0469 · Cited by 5

“Mitochondrial remodeling” in coronary heart disease

Saotome, M., Katoh, H., Satoh, H., Hayashi, H., & Hajnóczky, G. (2014) · Research Reports in Clinical Cardiology · doi:10.2147/rrcc.s43364 · Cited by 5

The role of cyclophilin D in interspecies differences in susceptibility to hepatotoxic drug-induced mitochondrial injury

Sekine, S., Kimura, T., Motoyama, M., Shitara, Y., Wakazono, H., Oida, H., & Horie, T. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.08.027 · Cited by 4

Cardioprotective Effects of S-Nitrosothiols in Ischemia- Reperfusion: Role for Mitochondria and Calcium Channels

Arriagada, O., Treuer, A. V., & González, D. R. (2018) · InTech eBooks · doi:10.5772/intechopen.77003 · Cited by 4

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

Jonas, E. A., Porter, G. A., Beutner, G., Mnatsakanyan, N., Park, H., Mehta, N. A., Chen, R., & Alavian, K. N. (2017) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-55539-3_3 · Cited by 4

Mitochondrial Regulators of Synaptic Plasticity in the Ischemic Brain

Park, H., & Jonas, E. A. (2017) · InTech eBooks · doi:10.5772/67126 · Cited by 4

Necrosis: Molecular Mechanisms and Physiological Roles

Duprez, L., Vanlangenakker, N., Festjens, N., Herreweghe, F. V., Berghe, T. V., & Vandenabeele, P. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-381-7_27 · Cited by 4

PLCδ1 Protein Rescues Ischemia-reperfused Heart by the Regulation of Calcium Homeostasis

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Endoplasmic Reticulum-mitochondria connections, calcium cross-talk and cell fate: a closer inspection

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