Molecular nature and regulation of the mitochondrial permeability transition pore(s), drug target(s) in cardioprotection

Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116 · see citing works

Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works

Mechanisms by which mitochondria transport calcium

Gunter, T. E., & Pfeiffer, D. R. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.258.5.c755 · Cited by 1,640 · see citing works

Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation

Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635 · see citing works

Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death

Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635 · see citing works

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works

Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury

Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,472 · see citing works

Effect of Cyclosporine on Reperfusion Injury in Acute Myocardial Infarction

Piot, C. A., Croisille, P., Staat, P., Thibault, H., Rioufol, G., Mewton, N., Belghiti, R. E., Cung, T. T., Bonnefoy‐Cudraz, E., Angoulvant, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa071142 · Cited by 1,339 · see citing works

Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria

Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works

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

Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · see citing works

Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside

Pebay‐Peyroula, E., Dahout-Gonzalez, C., Kahn, R., Trézéguet, V., Lauquin, G. J. ‐., & Brandolin, G. (2003) · Nature · doi:10.1038/nature02056 · Cited by 998 · see citing works

Mechanism of Fatty-Acid-Dependent UCP1 Uncoupling in Brown Fat Mitochondria

Fedorenko, A., Lishko, P. V., & Kirichok, Y. (2012) · Cell · doi:10.1016/j.cell.2012.09.010 · Cited by 968 · see citing works

Dimers of mitochondrial ATP synthase form the permeability transition pore

Giorgio, V., von Stockum, S., Antoniel, M., Fabbro, A., Fogolari, F., Forte, M. A., Glick, G. D., Petronilli, V., Zoratti, M., Szabó, I., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217823110 · Cited by 924 · see citing works

The Ca2+-induced membrane transition in mitochondria

Hunter, D. R., & Haworth, R. A. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90371-0 · Cited by 860 · see citing works

Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress.

Crompton, M., Ellinger, H., & COSTI, A. (1988) · PubMed Central · Cited by 841 · see citing works

Mitochondrial permeability transition and oxidative stress

Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02316-x · Cited by 832 · see citing works

Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease

Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826 · see citing works

Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia

Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., Hetz, C., Danial, N. N., Moskowitz, M. A., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505294102 · Cited by 820 · see citing works

The ATP synthase is involved in generating mitochondrial cristae morphology

Paumard, P., Vaillier, J., Coulary, B., Schaëffer, J., Soubannier, V., Mueller, D. M., Brèthes, D., di Rago, J., & Velours, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.221 · Cited by 809 · see citing works

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

Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · see citing works

The Ca2+-induced membrane transition in mitochondria

Haworth, R. A., & Hunter, D. R. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90372-2 · Cited by 793 · see citing works

Mitochondria Are Excitable Organelles Capable of Generating and Conveying Electrical and Calcium Signals

Ichas, F., Jouaville, L. S., & Mazat, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80301-3 · Cited by 754 · see citing works

Inhibition of Ca2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase

Halestrap, A. P., & Davidson, A. M. (1990) · Biochemical Journal · doi:10.1042/bj2680153 · Cited by 753 · see citing works

Calcineurin: a calcium- and calmodulin-binding protein of the nervous system.

Klee, C. B., Crouch, T. H., & Krinks, M. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.12.6270 · Cited by 738 · see citing works

Keilin's Respiratory Chain Concept and Its Chemiosmotic Consequences

Mitchell, P. (1979) · Science · doi:10.1126/science.388618 · Cited by 738 · see citing works

Cyclosporine before PCI in Patients with Acute Myocardial Infarction

Cung, T.-T., Morel, O., Cayla, G., Rioufol, G., Garcia-Dorado, D., Angoulvant, D., Bonnefoy-Cudraz, E., Guérin, P., Elbaz, M., Delarche, N., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1505489 · Cited by 713 · see citing works

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

Broekemeier, K. M., Dempsey, M. E., & Pfeiffer, D. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83116-7 · Cited by 699 · see citing works

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

Di Lisa, F., Menabò, R., Canton, M., Barile, M., & Bernardi, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006825200 · Cited by 678 · see citing works

Transient and Long-Lasting Openings of the Mitochondrial Permeability Transition Pore Can Be Monitored Directly in Intact Cells by Changes in Mitochondrial Calcein Fluorescence

Petronilli, V., Miotto, G., Canton, M., Brini, M., Colonna, R., Bernardi, P., & Lisa, F. D. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77239-5 · Cited by 677 · see citing works

Dimer ribbons of ATP synthase shape the inner mitochondrial membrane

Strauss, M., Hofhaus, G., Schröder, R. R., & Kühlbrandt, W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.35 · Cited by 677 · see citing works

The mitochondrial permeability transition from<i>in vitro</i>artifact to disease target

Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627 · see citing works

An uncoupling channel within the c-subunit ring of the F 1 F O ATP synthase is the mitochondrial permeability transition pore

Alavian, K. N., Beutner, G., Lazrove, E., Sacchetti, S., Park, H., Licznerski, P., Li, H., Nabili, P., Hockensmith, K., Graham, M. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401591111 · Cited by 595 · see citing works

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

Griffiths, E. J., & Halestrap, A. P. (1993) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1993.1162 · Cited by 587 · see citing works

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology

Bernardi, P., Rasola, A., Forte, M. A., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 586 · see citing works

Postconditioning Inhibits Mitochondrial Permeability Transition

Argaud, L., Gateau-Roesch, O., Raisky, O., Loufouat, J., Robert, D., & Ovize, M. (2005) · Circulation · doi:10.1161/01.cir.0000151290.04952.3b · Cited by 561 · see citing works

New roles for mitochondrial proteases in health, ageing and disease

Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works

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

Petronilli, V., Costantini, P., Scorrano, L., Colonna, R., Passamonti, S., & Bernardi, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89437-1 · Cited by 531 · see citing works

Macromolecular organization of ATP synthase and complex I in whole mitochondria

Davies, K. M., Strauss, M., Daum, B., Kief, J. H., Osiewacz, H. D., Ryčovská, A., Zickermann, V., & Kühlbrandt, W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103621108 · Cited by 526 · see citing works

Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency

Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works

Postconditioning and protection from reperfusion injury: where do we stand?Position Paper from the Working Group of Cellular Biology of the Heart of the European Society of Cardiology

Ovize, M., Baxter, G. F., Lisa, F. D., Ferdinandy, P., David Garcia-dorado, A., Hausenloy, D. J., Heusch, G., Vinten-Johansen, J., Yellon, D. M., & Schulz, R. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq129 · Cited by 502 · see citing works

The mitochondrial permeability transition pore: Molecular nature and role as a target in cardioprotection

Bernardi, P., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 499 · see citing works

Cyclophilin‐D binds strongly to complexes of the voltage‐dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore

Crompton, M., Virji, S., & Ward, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580729.x · Cited by 492 · see citing works

Interactions of Cyclophilin with the Mitochondrial Inner Membrane and Regulation of the Permeability Transition Pore, a Cyclosporin A-sensitive Channel

Nicolli, A., Basso, E., Petronilli, V., Wenger, R. M., & Bernardi, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.2185 · Cited by 482 · see citing works

The Mitochondrial Permeability Transition, Release of Cytochrome c and Cell Death

Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P., & Di Lisa, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010604200 · Cited by 472 · see citing works

The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal

Bernardi, P., & Petronilli, V. (1996) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110643 · Cited by 467 · see citing works

The Ca2+-induced membrane transition in mitochondria

Hunter, D. R., & Haworth, R. A. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90373-4 · Cited by 459 · see citing works

Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition

Bonora, M., Bononi, A., Marchi, E. D., Giorgi, C., Lebiedzińska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 454 · see citing works

Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations.

Bernardi, P., Vassanelli, S., Veronese, P., Colonna, R., Szabó, I., & Zoratti, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50676-7 · Cited by 453 · see citing works

Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization.

Bernardi, P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50355-6 · Cited by 449 · see citing works

Transient Opening of the Mitochondrial Permeability Transition Pore Induces Microdomain Calcium Transients in Astrocyte Processes

Agarwal, A., Wu, P.-H., Hughes, E. G., Fukaya, M., Tischfield, M. A., Langseth, A. J., Wirtz, D., & Bergles, D. E. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.034 · Cited by 441 · see citing works

Structure and Mechanisms of F-Type ATP Synthases

Kühlbrandt, W. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110903 · Cited by 438 · see citing works

Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function?

He, L., & Lemasters, J. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03314-2 · Cited by 435 · see citing works

Mitochondrial ADP/ATP Carrier Can Be Reversibly Converted into a Large Channel by Ca 2+

Brustovetsky, N., & Klingenberg, M. (1996) · Biochemistry · doi:10.1021/bi960833v · Cited by 423 · see citing works

The SLC25 Mitochondrial Carrier Family: Structure and Mechanism

Ruprecht, J. J., & Kunji, E. R. S. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.11.001 · Cited by 400 · see citing works

The mitochondrial Na+/Ca2+ exchanger is essential for Ca2+ homeostasis and viability

Luongo, T. S., Lambert, J. P., Gross, P., Nwokedi, M., Lombardi, A. A., Shanmughapriya, S., Carpenter, A. C., Kolmetzky, D., Gao, E., van Berlo, J. H., et al. (2017) · Nature · doi:10.1038/nature22082 · Cited by 396 · see citing works

Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition

Woodfield, K., Rück, A., Brdiczka, D. G., & Halestrap, A. P. (1998) · Biochemical Journal · doi:10.1042/bj3360287 · Cited by 386 · see citing works

Cyclophilin D controls mitochondrial pore–dependent Ca2+ exchange, metabolic flexibility, and propensity for heart failure in mice

Elrod, J. W., Wong, R., Mishra, S., Vagnozzi, R. J., Sakthievel, B., Goonasekera, S. A., Karch, J., Gabel, S., Farber, J., Force, T., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43171 · Cited by 384 · see citing works

Sanglifehrin A Acts as a Potent Inhibitor of the Mitochondrial Permeability Transition and Reperfusion Injury of the Heart by Binding to Cyclophilin-D at a Different Site from Cyclosporin A

Clarke, S. J., McStay, G. P., & Halestrap, A. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202191200 · Cited by 376 · see citing works

The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A

Szabó, I., & Zoratti, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67802-6 · Cited by 371 · see citing works

The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane.

Aquila, H., Link, T. A., & Klingenberg, M. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03941.x · Cited by 368 · see citing works

Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore

McSTAY, G. P., CLARKE, S. J., & HALESTRAP, A. P. (2002) · Biochemical Journal · doi:10.1042/bj20011672 · Cited by 367 · see citing works

Transient mitochondrial permeability transition pore opening mediates preconditioning-induced protection

Hausenloy, D., Wynne, A., Duchen, M., & Yellon, D. (2004) · Circulation · doi:10.1161/01.cir.0000126294.81407.7d · Cited by 366 · see citing works

Ischaemic Preconditioning Inhibits Opening of Mitochondrial Permeability Transition Pores in the Reperfused Rat Heart

Javadov, S. A., Clarke, S. J., Das, M., Griffiths, E. J., Lim, K. H. H., & Halestrap, A. P. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.034231 · Cited by 350 · see citing works

Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28

Bella, D. D., Lazzaro, F., Brusco, A., Plumari, M., Battaglia, G. S., Pastore, A., Finardi, A., Cagnoli, C., Tempia, F., Frontali, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.544 · Cited by 345 · see citing works

Action of cyclosporine on mitochondrial calcium fluxes

Fournier, N., Ducet, G., & Crevat, A. D. (1987) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762419 · Cited by 340 · see citing works

Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore

Beutner, G., Rück, A., Riede, B., Welte, W., & Brdiczka, D. G. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01092-7 · Cited by 337 · see citing works

Normalization of NAD + Redox Balance as a Therapy for Heart Failure

Lee, C. F., Chavez, J. D., Garcia‐Menendez, L., Choi, Y. S., Roe, N. D., Chiao, Y. A., Edgar, J. S., Goo, Y. A., Goodlett, D. R., Bruce, J. E., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022495 · Cited by 337 · see citing works

The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier

Ruprecht, J. J., King, M. S., Zögg, T., Aleksandrova, A. A., Pardon, E., Crichton, P. G., Steyaert, J., & Kunji, E. R. S. (2019) · Cell · doi:10.1016/j.cell.2018.11.025 · Cited by 321 · see citing works

Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria.

Petronilli, V., Cola, C., Massari, S., Colonna, R., & Bernardi, P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80631-0 · Cited by 317 · see citing works

The Mitochondrial Phosphate Carrier Interacts with Cyclophilin D and May Play a Key Role in the Permeability Transition

Leung, A. W. C., Varanyuwatana, P., & Halestrap, A. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805235200 · Cited by 315 · see citing works

Direct inhibition of the mitochondrial permeability transition pore: a possible mechanism responsible for anti‐apoptotic effects of melatonin

Andrabi, S. A., Sayeed, I., Siemen, D., Wolf, G. L., & Horn, T. F. W. (2004) · The FASEB Journal · doi:10.1096/fj.03-1031fje · Cited by 311 · see citing works

Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex

Giorgio, V., Bisetto, E., Soriano, M. E., Dabbeni‐Sala, F., Basso, E., Petronilli, V., Forte, M. A., Bernardi, P., & Lippe, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.020115 · Cited by 306 · see citing works

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM

Zhou, A., Rohou, A. L., Schep, D. G., Bason, J. V., Montgomery, M. G., Walker, J. E., Grigorieff, N., & Rubinstein, J. L. (2015) · eLife · doi:10.7554/elife.10180 · Cited by 298 · see citing works

On the involvement of a cyclosporin A sensitive mitochondrial pore in myocardial reperfusion injury

Duchen, M. R., McGuinness, O. M., Brown, L. A., & Crompton, M. (1993) · Cardiovascular Research · doi:10.1093/cvr/27.10.1790 · Cited by 294 · see citing works

Inhibition of the Mitochondrial Permeability Transition by the Nonimmunosuppressive Cyclosporin Derivative NIM811

Waldmeier, P. C., Feldtrauer, J.-J., Qian, T., & Lemasters, J. J. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.1.22 · Cited by 288 · see citing works

Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia

Atorino, L., Silvestri, L., Koppen, M., Cassina, L., Ballabio, A., Marconi, R., Langer, T., & Casari, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304112 · Cited by 283 · see citing works

The non‐immunosuppressive cyclosporin DEBIO‐025 is a potent inhibitor of hepatitis C virus replication in vitro†

Paeshuyse, J., Kaul, A., Clercq, E. D., Rosenwirth, B., Dumont, J., Scalfaro, P., Bartenschlager, R. F. W., & Neyts, J. H. (2006) · Hepatology · doi:10.1002/hep.21102 · Cited by 280 · see citing works

INACTIVATION OF OXIDATIVE AND PHOSPHORYLATIVE SYSTEMS IN MITOCHONDRIA BY PREINCUBATION WITH PHOSPHATE AND OTHER IONS

Hunter, F. E., & Ford, L. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52312-2 · Cited by 279 · see citing works

The mitochondrial megachannel is the permeability transition pore

Szab�, I., & Zoratti, M. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00769537 · Cited by 274 · see citing works

Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology

Hahn, A. S., Parey, K., Bublitz, M., Mills, D. J., Zickermann, V., Vonck, J., Kühlbrandt, W., & Meier, T. W. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.037 · Cited by 272 · see citing works

An Endogenous Uncoupling and Swelling Agent in Liver Mitochondria and Its Enzymic Formation

Lehninger, A. L., & Remmert, L. F. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69835-7 · Cited by 269 · see citing works

Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore

HüSER, J., & BLATTER, L. A. (1999) · Biochemical Journal · doi:10.1042/bj3430311 · Cited by 266 · see citing works

H+ transport is an integral function of the mitochondrial ADP/ATP carrier

Bertholet, A. M., Chouchani, E. T., Kazak, L., Angelin, A., Fedorenko, A., Long, J. Z., Vidoni, S., Garrity, R., Cho, J., Terada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1400-3 · Cited by 256 · see citing works

Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase

He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251 · see citing works

Inhibition of mitochondrial permeability transition by deletion of the ANT family and CypD

Karch, J., Bround, M. J., Khalil, H., Sargent, M. A., Latchman, N., Terada, N., Peixoto, P. M., & Molkentin, J. D. (2019) · Science Advances · doi:10.1126/sciadv.aaw4597 · Cited by 250 · see citing works

Modulation of the mitochondrial megachannel by divalent cations and protons.

Szabó, I., Bernardi, P., & Zoratti, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50677-9 · Cited by 241 · see citing works

The inner mitochondrial membrane contains ion‐conducting channels similar to those found in bacteria

Petronilli, V., Szabó, I., & Zoratti, M. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81513-3 · Cited by 238 · see citing works

The Mitochondrial Permeability Transition Pore is Modulated by Oxidative Agents Through Both Pyridine Nucleotides and Glutathione at Two Separate Sites

Chernyak, B. V., & Bernardi, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0623w.x · Cited by 233 · see citing works

Mechanism of mitochondrial permeability transition pore induction and damage in the pancreas: inhibition prevents acute pancreatitis by protecting production of ATP

Mukherjee, R., Mareninova, O. A., Odinokova, I. V., Huang, W., Murphy, J., Chvanov, M., Javed, M. A., Wen, L., Booth, D. M., Cane, M. C., et al. (2015) · Gut · doi:10.1136/gutjnl-2014-308553 · Cited by 233 · see citing works

Reversal of Various Types of Mitochondrial Swelling by Adenosine Triphosphate

Lehninger, A. L. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69836-9 · Cited by 227 · see citing works

The cyclophilin inhibitor Debio 025 combined with PEG IFNα2a significantly reduces viral load in treatment-naïve hepatitis C patients #

Flisiak, R., Feinman, S. V., Jabłkowski, M., Horban, A., Kryczka, W., Pawłowska, M., Heathcote, J., Mazzella, G., Vandelli, C., Nicolas‐Métral, V., et al. (2009) · Hepatology · doi:10.1002/hep.22835 · Cited by 227 · see citing works

Formation and disappearance of an endogenous uncoupling factor during swelling and contraction of mitochondria

Wojtczak, L., & Lehninger, A. L. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90600-x · Cited by 226 · see citing works

Inhibition of the mitochondrial permeability transition by cyclosporin A during long time frame experiments: relationship between pore opening and the activity of mitochondrial phospholipases

Broekemeier, K. M., & Pfeiffer, D. R. (1995) · Biochemistry · doi:10.1021/bi00050a027 · Cited by 225 · see citing works

Atomic model for the dimeric F _O region of mitochondrial ATP synthase

Guo, H., Bueler, S. A., & Rubinstein, J. L. (2017) · Science · doi:10.1126/science.aao4815 · Cited by 225 · see citing works

Mitochondrial channel activity studied by patch-clamping mitoplasts

Kinnally, K. W., Campo, M. L., & Tedeschi, H. (1989) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762521 · Cited by 223 · see citing works

Mitochondrial Ca2+ and regulation of the permeability transition pore

Hurst, S., Hoek, J. B., & Sheu, S. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9672-x · Cited by 220 · see citing works

Ca2+ binding to F‐ATP synthase β subunit triggers the mitochondrial permeability transition

Giorgio, V., Burchell, V., Schiavone, M., Bassot, C., Minervini, G., Petronilli, V., Argenton, F., Forte, M. A., Tosatto, S. C. E., Lippe, G., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643354 · Cited by 214 · see citing works

Regulation of the permeability transition pore, a voltage-dependent mitochondrial channel inhibited by cyclosporin A

Petronilli, V., Nicolli, A., Costantini, P., Colonna, R., & Bernardi, P. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90122-8 · Cited by 210 · see citing works

SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore

Shanmughapriya, S., Rajan, S., Hoffman, N. E., Higgins, A. M., Tomar, D., Nemani, N., Hines, K. J., Smith, D. J., Eguchi, A., Vallem, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.009 · Cited by 209 · see citing works

The m -AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria

König, T., Tröder, S. E., Bakka, K., Korwitz, A., Richter‐Dennerlein, R., Lampe, P., Patrón, M., Mühlmeister, M., Guerrero‐Castillo, S., Brandt, U., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.020 · Cited by 201 · see citing works

Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1

Gu, J., Zhang, L., Zong, S., Guo, R., Liu, T., Yi, J., Wang, P., Zhuo, W., & Yang, M. (2019) · Science · doi:10.1126/science.aaw4852 · Cited by 197 · see citing works

Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore. I. Evidence for two separate Me2+ binding sites with opposing effects on the pore open probability.

Bernardi, P., Veronese, P., & Petronilli, V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54033-3 · Cited by 196 · see citing works

The mitochondrial permeability transition pore may comprise VDAC molecules

Szabó, I., & Zoratti, M. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80273-w · Cited by 192 · see citing works

Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by matrix pH. Evidence that the pore open-closed probability is regulated by reversible histidine protonation

Nicolli, A., Petronilli, V., & Bernardi, P. (1993) · Biochemistry · doi:10.1021/bi00067a039 · Cited by 192 · see citing works

Calcium and regulation of the mitochondrial permeability transition

Giorgio, V., Guo, L., Bassot, C., Petronilli, V., & Bernardi, P. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.05.004 · Cited by 191 · see citing works

Intramitochondrial phospholipase activity and the effects of Ca2+ plus N-ethylmaleimide on mitochondrial function.

Pfeiffer, D. R., Schmid, P. C., Beatrice, M. C., & Schmid, H. H. O. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86511-0 · Cited by 189 · see citing works

ATP Synthase C-Subunit-Deficient Mitochondria Have a Small Cyclosporine A-Sensitive Channel, but Lack the Permeability Transition Pore

Neginskaya, M. A., Solesio, M. E., Berezhnaya, E. V., Amodeo, G. F., Mnatsakanyan, N., Jonas, E. A., & Pavlov, E. V. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.033 · Cited by 187 · see citing works

Structure of dimeric mitochondrial ATP synthase: Novel F 0 bridging features and the structural basis of mitochondrial cristae biogenesis

Minauro‐Sanmiguel, F., Wilkens, S., & García, J. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503893102 · Cited by 186 · see citing works

Mitochondrial Permeability Transition: A Molecular Lesion with Multiple Drug Targets

Briston, T., Selwood, D. L., Szabadkai, G., & Duchen, M. R. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.11.004 · Cited by 185 · see citing works

Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore

Urbani, A., Giorgio, V., Carrer, A., Franchin, C., Arrigoni, G., Jiko, C., Abe, K., Maeda, S., Shinzawa‐Itoh, K., Bogers, J. F. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12331-1 · Cited by 183 · see citing works

Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase

He, J., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711201114 · Cited by 182 · see citing works

Preconditioning delays Ca2+-induced mitochondrial permeability transition

Argaud, L. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.11.003 · Cited by 180 · see citing works

On the Voltage Dependence of the Mitochondrial Permeability Transition Pore

Scorrano, L., Petronilli, V., & Bernardi, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12295 · Cited by 178 · see citing works

Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy

Kwong, J. Q., Davis, J., Baines, C. P., Sargent, M. A., Karch, J., Wang, X., Huang, T., & Molkentin, J. D. (2014) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2014.36 · Cited by 174 · see citing works

NIM811, a Cyclophilin Inhibitor, Exhibits Potent In Vitro Activity against Hepatitis C Virus Alone or in Combination with Alpha Interferon

Ma, S., Boerner, J. E., Tiong-Yip, C.-L., Weidmann, B., Ryder, N. S., Cooreman, M. P., & Lin, K. W. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00310-06 · Cited by 164 · see citing works

Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition

Carraro, M., Giorgio, V., Šileikytė, J., Sartori, G., Forte, M. A., Lippe, G., Zoratti, M., Szabó, I., & Bernardi, P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.559633 · Cited by 160 · see citing works

A mitochondrial megachannel resides in monomeric F1FO ATP synthase

Mnatsakanyan, N., Llaguno, M. C., Yang, Y., Yan, Y., Weber, J., Sigworth, F. J., & Jonas, E. A. (2019) · Nature Communications · doi:10.1038/s41467-019-13766-2 · Cited by 152 · see citing works

Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore

Rück, A., Dolder, M., Wallimann, T., & Brdiczka, D. G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00317-2 · Cited by 151 · see citing works

The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function

Quintana–Cabrera, R., Quirin, C., Glytsou, C., Corrado, M., Urbani, A., Pellattiero, A., Calvo, E., Vázquez, J., Enrı́quez, J. A., Gerle, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05655-x · Cited by 150 · see citing works

Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria

Dudkina, N. V., Sunderhaus, S., Braun, H., & Boekema, E. J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.097 · Cited by 145 · see citing works

The Nonimmunosuppressive Cyclosporin Analogs NIM811 and UNIL025 Display Nanomolar Potencies on Permeability Transition in Brain-Derived Mitochondria

Hansson, M. J., Mattiasson, G., Månsson, R., Karlsson, J., Keep, M. F., Waldmeier, P. C., Rüegg, U. T., Dumont, J., Besseghir, K., & Elmér, E. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041776.31885.45 · Cited by 141 · see citing works

Physiological cytosolic Ca2+ transients evoke concurrent mitochondrial depolarizations.

Loew, L. M., Carrington, W., Tuft, R. A., & Fay, F. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12579 · Cited by 140 · see citing works

Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity

Yamaguchi, R., Andreyev, A. Y., Murphy, A. N., Perkins, G. A., Ellisman, M. H., & Newmeyer, D. D. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402035 · Cited by 135 · see citing works

A Large, Voltage-Dependent Channel, Isolated from Mitochondria by Water-Free Chloroform Extraction

Pavlov, E. V., Zakharian, E., Bladen, C., Diao, C. T. M., Grimbly, C., Reusch, R. N., & French, R. J. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.057281 · Cited by 134 · see citing works

A research journey with ATP synthase

Boyer, P. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.x200001200 · Cited by 130 · see citing works

A Large Ca 2+ -Dependent Channel Formed by Recombinant ADP/ATP Carrier from Neurospora crassa Resembles the Mitochondrial Permeability Transition Pore

Brustovetsky, N., Tropschug, M., Heimpel, S., Heidkaemper, D., & Klingenberg, M. (2002) · Biochemistry · doi:10.1021/bi0200110 · Cited by 128 · see citing works

Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase

Carroll, J., He, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904005116 · Cited by 128 · see citing works

Identification and Validation of the Mitochondrial F1F0-ATPase as the Molecular Target of the Immunomodulatory Benzodiazepine Bz-423

Johnson, K. M., Chen, X., Boitano, A. E., Swenson, L., Opipari, A. W., & Glick, G. D. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.02.012 · Cited by 127 · see citing works

The unique histidine in OSCP subunit of F‐ATP synthase mediates inhibition of the permeability transition pore by acidic pH

Antoniel, M., Jones, K., Antonucci, S., Spolaore, B., Fogolari, F., Petronilli, V., Giorgio, V., Carraro, M., Lisa, F. D., Forte, M. A., et al. (2017) · EMBO Reports · doi:10.15252/embr.201744705 · Cited by 124 · see citing works

The cyclophilin inhibitor Debio 025 normalizes mitochondrial function, muscle apoptosis and ultrastructural defects inCol6a1−/−myopathic mice

Tiepolo, T., Angelin, A., Palma, E., Sabatelli, P., Merlini, L., Nicolosi, L., Finetti, F., Braghetta, P., Vuagniaux, G., Dumont, J., et al. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00316.x · Cited by 121 · see citing works

Dual role for the ADP/ATP translocator?

Halestrap, A. P. (2004) · Nature · doi:10.1038/nature02816 · Cited by 121 · see citing works

Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM

Baker, L. A., Watt, I. N., Runswick, M. J., Walker, J. E., & Rubinstein, J. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204935109 · Cited by 120 · see citing works

Inhibition of Drp1-dependent mitochondrial fragmentation and apoptosis by a polypeptide antagonist of calcineurin

Cereghetti, G. M., Costa, V., & Scorrano, L. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.61 · Cited by 116 · see citing works

From ATP to PTP and Back

Bernardi, P., Lisa, F. D., Fogolari, F., & Lippe, G. (2015) · Circulation Research · doi:10.1161/circresaha.115.306557 · Cited by 113 · see citing works

Inhibition of Human Immunodeficiency Virus Type 1 Replication in Human Cells by Debio-025, a Novel Cyclophilin Binding Agent

Ptak, R. G., Gallay, P. A., Jochmans, D., Halestrap, A. P., Rüegg, U. T., Pallansch, L. A., Bobardt, M. D., de Béthune, M., Neyts, J. H., Clercq, E. D., et al. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01324-07 · Cited by 112 · see citing works

Identification of Two Proteins Associated with Mammalian ATP Synthase

Meyer, B., Wittig, I., Trifilieff, É., Karas, M., & Schägger, H. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700097-mcp200 · Cited by 112 · see citing works

Individual Cardiac Mitochondria Undergo Rare Transient Permeability Transition Pore Openings

Lu, X., Kwong, J. Q., Molkentin, J. D., & Bers, D. M. (2015) · Circulation Research · doi:10.1161/circresaha.115.308093 · Cited by 109 · see citing works

The Voltage-dependent Anion Channel Is the Target for a New Class of Inhibitors of the Mitochondrial Permeability Transition Pore

Cesura, A. M., Pinard, E., Schubenel, R., Goetschy, V., Friedlein, A., Langen, H., Polčic, P., Forte, M. A., Bernardi, P., & Kemp, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304748200 · Cited by 107 · see citing works

The equivalent pore radius of intact and damaged mitochondria and the mechanism of active shrinkage

Massari, S., & AZZONE, G. F. (1972) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(72)90094-1 · Cited by 106 · see citing works

Compartmentalization of a unique ADP/ATP carrier protein SFEC (Sperm Flagellar Energy Carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece

Kim, Y.-H., Haidl, G., Schäfer, M., Egner, U., Mandal, A., & Herr, J. C. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.10.004 · Cited by 106 · see citing works

Sanglifehrin A, a Novel Cyclophilin-Binding Compound Showing Immunosuppressive Activity with a New Mechanism of Action

Zenke, G., Strittmatter, U., Fuchs, S., Quesniaux, V. F. J., Brinkmann, V., Schüler, W., Zurini, M. G. M., Enz, A., Billich, A., Sanglier, J., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7165 · Cited by 105 · see citing works

GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM

Hauer, F., Gerle, C., Fischer, N., Oshima, A., Shinzawa‐Itoh, K., Shimada, S., Yokoyama, K., Fujiyoshi, Y., & Stark, H. (2015) · Structure · doi:10.1016/j.str.2015.06.029 · Cited by 104 · see citing works

Investigation of Debio 025, a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy

Reutenauer, J., Dorchies, O. M., Patthey-Vuadens, O., Vuagniaux, G., & Rüegg, U. T. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.285 · Cited by 102 · see citing works

Clinically Approved Heterocyclics Act on a Mitochondrial Target and Reduce Stroke-induced Pathology

Stavrovskaya, I. G., Narayanan, M. V., Zhang, W., Krasnikov, B. F., Heemskerk, J., Young, S. S., Blass, J. P., Brown, A. M., Beal, M. F., Friedlander, R. M., et al. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20032053 · Cited by 99 · see citing works

Maintenance of Energy-Linked Functions in Rat-Liver Mitochondria Aged in the Presence of Nupercaine

Scarpa, A., & LINDSAY, J. G. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb01851.x · Cited by 95 · see citing works

Free Fatty Acid Effects on Mitochondrial Permeability: An Overview

Sultan, A., & Sokolove, P. M. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2195 · Cited by 94 · see citing works

Selective inhibition of the mitochondrial permeability transition pore at the oxidation‐reduction sensitive dithiol by monobromobimane

Costantini, P., Chernyak, B. V., Petronilli, V., & Bernardi, P. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00256-9 · Cited by 88 · see citing works

Induction of the mitochondrial permeability transition by N-ethylmaleimide depends on secondary oxidation of critical thiol groups. Potentiation by copper-ortho-phenanthroline without dimerization of the adenine nucleotide translocase

Costantini, P., Colonna, R., & Bernardi, P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00090-5 · Cited by 88 · see citing works

Proteolytic control of the mitochondrial calcium uniporter complex

Tsai, C.-W., Wu, Y., Pao, P., Phillips, C. B., Williams, C., Miller, C., Ranaghan, M. J., & Tsai, M.-F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702938114 · Cited by 87 · see citing works

Activation of the mitochondrial permeability transition pore modulates Ca2+ responses to physiological stimuli in adult neurons

Barsukova, A. G., Komarov, A. G., Hajnóczky, G., Bernardi, P., BOURDETTE, D. N., & Forte, M. A. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07576.x · Cited by 86 · see citing works

ATP synthase oligomerization: From the enzyme models to the mitochondrial morphology

Habersetzer, J., Ziani, W., Larrieu, I., Stines‐Chaumeil, C., Giraud, M., Brèthes, D., Dautant, A., & Paumard, P. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.017 · Cited by 85 · see citing works

Diazoxide Opens the Mitochondrial Permeability Transition Pore and Alters Ca 2+ Transients in Rat Ventricular Myocytes

Katoh, H., Nishigaki, N., & Hayashi, H. (2002) · Circulation · doi:10.1161/01.cir.0000016831.41648.04 · Cited by 79 · see citing works

Immunochemical characterization of the adenine nucleotide translocator

Schultheiß, H., & Klingenberg, M. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08412.x · Cited by 78 · see citing works

Cinnamic Anilides as New Mitochondrial Permeability Transition Pore Inhibitors Endowed with Ischemia-Reperfusion Injury Protective Effect in Vivo

Fancelli, D., Abate, A., Amici, R., Bernardi, P., Ballarini, M., Cappa, A., Carenzi, G. E. A., Colombo, A., Contursi, C., Lisa, F. D., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500547c · Cited by 78 · see citing works

Atomistic simulations indicate the c-subunit ring of the F1Fo ATP synthase is not the mitochondrial permeability transition pore

Zhou, W., Marinelli, F., Nief, C., & Faraldo-Gómez, J. D. (2017) · eLife · doi:10.7554/elife.23781 · Cited by 75 · see citing works

Post-Injury Administration of the Mitochondrial Permeability Transition Pore Inhibitor, NIM811, Is Neuroprotective and Improves Cognition after Traumatic Brain Injury in Rats

Readnower, R. D., Pandya, J. D., McEwen, M. L., Pauly, J. R., Springer, J. E., & Sullivan, P. G. (2011) · Journal of Neurotrauma · doi:10.1089/neu.2011.1755 · Cited by 74 · see citing works

F-ATPase of Drosophila melanogaster Forms 53-Picosiemen (53-pS) Channels Responsible for Mitochondrial Ca2+-induced Ca2+ Release

von Stockum, S., Giorgio, V., Trevisan, E., Lippe, G., Glick, G. D., Forte, M. A., Da‐Ré, C., Checchetto, V., Mazzotta, G. M., Costa, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.629766 · Cited by 73 · see citing works

Cyclophilin D Promotes Brain Mitochondrial F1FO ATP Synthase Dysfunction in Aging Mice

Gauba, E., Guo, L., & Du, H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160822 · Cited by 73 · see citing works

Éxchange entre adenine-nucleotides extra- et intramitochondriaux

Duée, E. D., & Vignais, P. V. (1965) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(65)90419-8 · Cited by 72 · see citing works

NIM811, a cyclophilin inhibitor without immunosuppressive activity, is beneficial in collagen VI congenital muscular dystrophy models

Zulian, A., Rizzo, E., Schiavone, M., Palma, E., Tagliavini, F., Blaauw, B., Merlini, L., Maraldi, N. M., Sabatelli, P., Braghetta, P., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu254 · Cited by 72 · see citing works

High-Conductance Channel Formation in Yeast Mitochondria is Mediated by F-ATP Synthase e and g Subunits

Carraro, M., Checchetto, V., Sartori, G., Kucharczyk, R., di Rago, J., Minervini, G., Franchin, C., Arrigoni, G., Giorgio, V., Petronilli, V., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000494864 · Cited by 68 · see citing works

Dynamics of the mitochondrial permeability transition pore: Transient and permanent opening events

Boyman, L., Coleman, A. K., Zhao, G., Wescott, A. P., Joca, H. C., Greiser, B. M., Karbowski, M., Ward, C. W., & Lederer, W. J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.03.016 · Cited by 68 · see citing works

Structural changes in the transport cycle of the mitochondrial ADP/ATP carrier

Ruprecht, J. J., & Kunji, E. R. S. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.029 · Cited by 67 · see citing works

Debio-025 is more effective than prednisone in reducing muscular pathology in mdx mice

Wissing, E. R., Millay, D. P., Vuagniaux, G., & Molkentin, J. D. (2010) · Neuromuscular Disorders · doi:10.1016/j.nmd.2010.06.016 · Cited by 66 · see citing works

Alisporivir rescues defective mitochondrial respiration in Duchenne muscular dystrophy

Schiavone, M., Zulian, A., Menazza, S., Petronilli, V., Argenton, F., Merlini, L., Sabatelli, P., & Bernardi, P. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.09.001 · Cited by 66 · see citing works

Rapid Suppression of Mitochondrial Permeability Transition by Methylglyoxal

Speer, O., Morkūnaitė‐Haimi, Š., Liobikas, J., Franck, M. C. M., Hensbo, L., Linder, M. D., Kinnunen, P. K. J., Wallimann, T., & Eriksson, O. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301990200 · Cited by 64 · see citing works

GNX-4728, a novel small molecule drug inhibitor of mitochondrial permeability transition, is therapeutic in a mouse model of amyotrophic lateral sclerosis

Martin, L. J., Fancelli, D., Wong, M., Niedzwiecki, M. V., Ballarini, M., Plyte, S. E., & Chang, Q. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00433 · Cited by 63 · see citing works

On the structural possibility of pore-forming mitochondrial F o F 1 ATP synthase

Gerle, C. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.008 · Cited by 57 · see citing works

F‐ ATP synthase and the permeability transition pore: fewer doubts, more certainties

Carraro, M., Checchetto, V., Szabó, I., & Bernardi, P. (2019) · FEBS Letters · doi:10.1002/1873-3468.13485 · Cited by 57 · see citing works

Palmitic and Stearic Acids Bind Ca2+ with High Affinity and Form Nonspecific Channels in Black-Lipid Membranes. Possible Relation to Ca2+-Activated Mitochondrial Pores

Mironova, G. D., Gateau-Roesch, O., Levrat, C., Gritsenko, E. N., Pavlov, E. V., Lazareva, A. V., Limarenko, E. A., Rey, C., Louisot, P., & Saris, N.-E. L. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010659323937 · Cited by 56 · see citing works

Volume changes in liver mitochondria.

AZZONE, G. F., & Azzi, A. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.53.5.1084 · Cited by 56 · see citing works

Inhibition of Cell Cycle Progression by the Novel Cyclophilin Ligand Sanglifehrin A Is Mediated through the NFκB-dependent Activation of p53

Zhang, L.-H., Youn, H., & Liu, J. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104257200 · Cited by 55 · see citing works

Cyclophilin D deficiency attenuates mitochondrial F1Fo ATP synthase dysfunction via OSCP in Alzheimer's disease

Gauba, E., Chen, H., Guo, L., & Du, H. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.09.020 · Cited by 55 · see citing works

Discovery of Novel 1,3,8-Triazaspiro[4.5]decane Derivatives That Target the c Subunit of F1/FO-Adenosine Triphosphate (ATP) Synthase for the Treatment of Reperfusion Damage in Myocardial Infarction

Morciano, G., Preti, D., Pedriali, G., Aquila, G., Missiroli, S., Fantinati, A., Caroccia, N., Pacifico, S., Bonora, M., Talarico, A., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00278 · Cited by 54 · see citing works

Electrophysiological characterization of the Cyclophilin D-deleted mitochondrial permeability transition pore

Marchi, U. D., Basso, E., Szabó, I., & Zoratti, M. (2006) · Molecular Membrane Biology · doi:10.1080/09687860600907644 · Cited by 53 · see citing works

Molecular Mechanisms of Immunosuppression by Cyclosporins

Zenke, G., Baumann, G., Wenger, R. M., HIESTAND, P. C., Quesniaux, V. F. J., Andersen, E., & Schreier, M. H. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb35882.x · Cited by 53 · see citing works

Chemical Modification of Arginines by 2,3-Butanedione and Phenylglyoxal Causes Closure of the Mitochondrial Permeability Transition Pore

Eriksson, O., Fontaine, E. M., & Bernardi, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12669 · Cited by 51 · see citing works

Inhibition of Ca2+ efflux from mitochondria by nupercaine and tetracaine

Dawson, A. P., Selwyn, M. J., & FULTON, D. V. (1979) · Nature · doi:10.1038/277484a0 · Cited by 50 · see citing works

Protective Effects of NIM811 in Transient Focal Cerebral Ischemia Suggest Involvement of the Mitochondrial Permeability Transition

Korde, A. S., Pettigrew, L. C., Craddock, S. D., Pocernich, C. B., Waldmeier, P. C., & Maragos, W. F. (2007) · Journal of Neurotrauma · doi:10.1089/neu.2006.0122 · Cited by 48 · see citing works

Estrogen receptor beta modulates permeability transition in brain mitochondria

Burstein, S. R., Kim, H. J., Fels, J. A., Qian, L., Zhang, S., Zhou, P., Starkov, A. A., Iadecola, C., & Manfredi, G. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.03.006 · Cited by 48 · see citing works

Discovery, Synthesis, and Optimization of Diarylisoxazole‐3‐carboxamides as Potent Inhibitors of the Mitochondrial Permeability Transition Pore

Roy, S., Šileikytė, J., Schiavone, M., Neuenswander, B., Argenton, F., Aubé, J., Hedrick, M. P., Chung, T. D. Y., Forte, M. A., Bernardi, P., et al. (2015) · ChemMedChem · doi:10.1002/cmdc.201500284 · Cited by 47 · see citing works

Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal

Guo, L., Carraro, M., Sartori, G., Minervini, G., Eriksson, O., Petronilli, V., & Bernardi, P. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004495 · Cited by 47 · see citing works

lncRNA Structure: Message to the Heart

Fazal, F. M., & Chang, H. Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.030 · Cited by 46 · 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

Patch clamp investigation into the phosphate carrier from Saccharomyces cerevisiae mitochondria

Herick, K., Krämer, R., & Lühring, H. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00050-9 · Cited by 44 · see citing works

Structural Basis for the Non-Immunosuppressive Character of the Cyclosporin A Analogue Debio 025

Landrieu, I., Hanoulle, X., Bonachéra, F., Hamel, A., Sibille, N., Yin, Y., Wieruszeski, J., Horvath, D., Wei, Q., Vuagniaux, G., et al. (2010) · Biochemistry · doi:10.1021/bi1003266 · Cited by 43 · see citing works

Arg-8 of yeast subunit e contributes to the stability of F-ATP synthase dimers and to the generation of the full-conductance mitochondrial megachannel

Guo, L., Carraro, M., Carrer, A., Minervini, G., Urbani, A., Masgras, I., Tosatto, S. C. E., Szabó, I., Bernardi, P., & Lippe, G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008775 · Cited by 42 · see citing works

NMR studies of an immunomodulatory benzodiazepine binding to its molecular target on the mitochondrial F1F0‐ATPase

Stelzer, A. C., Frazee, R. W., Huis, C. V., Cleary, J., Opipari, A. W., Glick, G. D., & Al‐Hashimi, H. M. (2009) · Biopolymers · doi:10.1002/bip.21306 · Cited by 40 · see citing works

N‐Phenylbenzamides as Potent Inhibitors of the Mitochondrial Permeability Transition Pore

Roy, S., Šileikytė, J., Neuenswander, B., Hedrick, M. P., Chung, T. D. Y., Aubé, J., Schoenen, F. J., Forte, M. A., & Bernardi, P. (2015) · ChemMedChem · doi:10.1002/cmdc.201500545 · Cited by 40 · see citing works

Novel mitochondrial transition pore inhibitor N‐methyl‐4‐isoleucine cyclosporin is a new therapeutic option in acute pancreatitis

Tóth, E., Maléth, J., Závogyán, N., Fanczal, J., Grassalkovich, A., Erdős, R., Pallagi, P., Horváth, G., Tretter, L., Bálint, E. R., et al. (2019) · The Journal of Physiology · doi:10.1113/jp278517 · Cited by 40 · see citing works

Mechanisms for Ca 2+ -dependent permeability transition in mitochondria

Bernardi, P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921035117 · Cited by 39 · see citing works

Is there a common binding center in the ADP, ATP carrier for substrate and inhibitors?

Klingenberg, M., & Appel, M. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81029-5 · Cited by 37 · see citing works

Modification of Permeability Transition Pore Arginine(s) by Phenylglyoxal Derivatives in Isolated Mitochondria and Mammalian Cells

Johans, M., Milanesi, E., Franck, M. C. M., Johans, C., Liobikas, J., Panagiotaki, M., Greci, L., Principato, G., Kinnunen, P. K. J., Bernardi, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413454200 · Cited by 37 · see citing works

SPG7 targets the m-AAA protease complex to process MCU for uniporter assembly, Ca2+ influx, and regulation of mitochondrial permeability transition pore opening

Hurst, S., Baggett, A., Csordás, G., & Sheu, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006443 · Cited by 37 · see citing works

Deletion of Amino Acids 261−269 in the Brown Fat Uncoupling Protein Converts the Carrier into a Pore

González‐Barroso, M. M., Fleury, C., Lévi-Meyrueis, C., Zaragoza, P., Bouillaud, F., & Rial, E. (1997) · Biochemistry · doi:10.1021/bi971104y · Cited by 36 · see citing works

A novel class of cardioprotective small-molecule PTP inhibitors

Antonucci, S., Sante, M. D., Šileikytė, J., Devereaux, J., Bauer, T. M., Bround, M. J., Menabò, R., Paillard, M., Alánová, P., Carraro, M., et al. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104548 · Cited by 34 · see citing works

Mutations in the β-Subunit Thr159 and Glu184 of the Rhodospirillum rubrumF0F1 ATP Synthase Reveal Differences in Ligands for the Coupled Mg2+- and Decoupled Ca2+-dependent F0F1 Activities

Nathanson, L., & Gromet‐Elhanan, Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.901 · Cited by 33 · see citing works

Second‐Generation Inhibitors of the Mitochondrial Permeability Transition Pore with Improved Plasma Stability

Šileikytė, J., Devereaux, J., de Jong, J. C. B. C., Schiavone, M., Jones, K. L., Nilsen, A., Bernardi, P., Forte, M. A., & Cohen, M. S. (2019) · ChemMedChem · doi:10.1002/cmdc.201900376 · Cited by 31 · see citing works

Ligand-selective Modulation of the Permeability Transition Pore by Arginine Modification

Linder, M. D., Morkūnaitė‐Haimi, Š., Kinnunen, P. K. J., Bernardi, P., & Eriksson, O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107610200 · Cited by 30 · see citing works

Identification of ER-000444793, a Cyclophilin D-independent inhibitor of mitochondrial permeability transition, using a high-throughput screen in cryopreserved mitochondria

Briston, T., Lewis, S., Koglin, M., Mistry, K., Shen, Y., Hartopp, N., Katsumata, R., Fukumoto, H., Duchen, M. R., Szabadkai, G., et al. (2016) · Scientific Reports · doi:10.1038/srep37798 · Cited by 30 · see citing works

Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions

Bernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 482 · see citing works

Mitochondrial pores at the crossroad between cell death and inflammatory signaling

Flores‐Romero, H., Dadsena, S., & García‐Sáez, A. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.021 · Cited by 125 · see citing works

Mitochondrial dysfunction in cardiovascular disease: Current status of translational research/clinical and therapeutic implications

Manolis, A. S., Manolis, A. A., Manolis, T. A., Apostolaki, N. E., Apostolopoulos, E. J., Melita, H., & Katsiki, N. (2020) · Medicinal Research Reviews · doi:10.1002/med.21732 · Cited by 116 · see citing works

Ca2+ handling at the mitochondria-ER contact sites in neurodegeneration

Lim, D., Dematteis, G., Tapella, L., Genazzani, A. A., Calí, T., Brini, M., & Verkhratsky, A. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102453 · Cited by 105 · see citing works

The mitochondrial permeability transition: Nexus of aging, disease and longevity

Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works

Mitochondrial Ion Channels

Szabó, I., & Szewczyk, A. M. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-092622-094853 · Cited by 91 · see citing works

Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase

Carrer, A., Tommasin, L., Šileikytė, J., Ciscato, F., Filadi, R., Urbani, A., Forte, M. A., Rasola, A., Szabó, I., Carraro, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25161-x · Cited by 87 · see citing works

Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology

Nesci, S., Trombetti, F., Pagliarani, A., Ventrella, V., Algieri, C., Tioli, G., & Lenaz, G. (2021) · Life · doi:10.3390/life11030242 · Cited by 80 · see citing works

Targeting mitochondrial ion channels for cancer therapy

Szabó, I., Zoratti, M., & Biasutto, L. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101846 · Cited by 77 · see citing works

Asiatic Acid Alleviates Myocardial Ischemia‐Reperfusion Injury by Inhibiting the ROS‐Mediated Mitochondria‐Dependent Apoptosis Pathway

Yi, C., Song, M., Sun, L., Si, L., Yu, D., Li, B., Lü, P., Wang, W., & Wang, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3267450 · Cited by 70 · see citing works

Mitochondrial K+ channels and their implications for disease mechanisms

Checchetto, V., Leanza, L., Stefani, D. D., Rizzuto, R., Gulbins, E., & Szabó, I. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107874 · Cited by 57 · see citing works

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

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

Urbani, A., Prosdocimi, E., Carrer, A., Checchetto, V., & Szabó, I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.620081 · Cited by 49 · see citing works

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

Neginskaya, M. A., Pavlov, E. V., & Sheu, S. S. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148357 · Cited by 45 · see citing works

The Reduction in the Mitochondrial Membrane Potential in Aging: The Role of the Mitochondrial Permeability Transition Pore

Rottenberg, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512295 · Cited by 44 · see citing works

Calcium influx through the mitochondrial calcium uniporter holocomplex, MCUcx

Boyman, L., Greiser, M., & Lederer, W. J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.10.015 · Cited by 42 · see citing works

ATP Synthase K+- and H+-fluxes Drive ATP Synthesis and Enable Mitochondrial K+-“Uniporter” Function: II. Ion and ATP Synthase Flux Regulation

Juhaszova, M., Kobrinsky, E., Zorov, D. B., Nuss, H. B., Yaniv, Y., Fishbein, K. W., de Cabo, R., Montoliu, L., Gabelli, S. B., Aon, M. A., et al. (2022) · Function · doi:10.1093/function/zqac001 · Cited by 40 · see citing works

Mitochondrial Fission Process 1 controls inner membrane integrity and protects against heart failure

Donnarumma, E., Kohlhaas, M., Vimont, E., Kornobis, É., Chaze, T., Gianetto, Q. G., Matondo, M., Moya‐Nilges, M., Maack, C., & Wai, T. (2022) · Nature Communications · doi:10.1038/s41467-022-34316-3 · Cited by 40 · see citing works

The role of mitochondria in metabolic disease: a special emphasis on heart dysfunction

Federico, M., de la Fuente, S., Palomeque, J., & Sheu, S. (2021) · The Journal of Physiology · doi:10.1113/jp279376 · Cited by 37 · see citing works

Discovery and molecular basis of subtype-selective cyclophilin inhibitors

Peterson, A. A., Rangwala, A. M., Thakur, M. K., Ward, P. S., Hung, C., Outhwaite, I. R., Chan, A. I., Usanov, D. L., Mootha, V. K., Seeliger, M. A., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01116-1 · Cited by 37 · see citing works

Treatment with a triazole inhibitor of the mitochondrial permeability transition pore fully corrects the pathology of sapje zebrafish lacking dystrophin

Stocco, A., Smolina, N., Sabatelli, P., Šileikytė, J., Artusi, E., Mouly, V., Cohen, M. S., Forte, M. A., Schiavone, M., & Bernardi, P. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105421 · Cited by 36 · see citing works

DJ-1: A promising therapeutic candidate for ischemia-reperfusion injury

Lazzari, F. D., Prag, H. A., Gruszczyk, A. V., Whitworth, A. J., & Bisaglia, M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101884 · Cited by 36 · see citing works

ANT2 drives proinflammatory macrophage activation in obesity

Moon, J.-S., da Cunha, F. F., Huh, J. Y., Andreyev, A. Y., Lee, J., Mahata, S. K., Reis, F. C. G., Nasamran, C. A., & Lee, Y. S. (2021) · JCI Insight · doi:10.1172/jci.insight.147033 · Cited by 35 · see citing works

ATP synthase FOF1 structure, function, and structure-based drug design

Vlasov, A. V., Osipov, S. D., Bondarev, N. A., Uversky, V. N., Borshchevskiy, V. I., Yanyushin, M. F., Манухов, И. В., Rogachev, A. V., Vlasova, A. D., Ilyinsky, N. S., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04153-0 · Cited by 34 · see citing works

Mitochondrial sirtuins, key regulators of aging

Ji, Z., Liu, G., & Qu, J. T. (2025) · Life Medicine · doi:10.1093/lifemedi/lnaf019 · Cited by 31 · see citing works

Comparison of Effects of Metformin, Phenformin, and Inhibitors of Mitochondrial Complex I on Mitochondrial Permeability Transition and Ischemic Brain Injury

Škėmienė, K., Rekuvienė, E., Jekabsone, A., Čižas, P., Morkūnienė, R., & Borutaitė, V. (2020) · Biomolecules · doi:10.3390/biom10101400 · Cited by 30 · see citing works

Mitochondrial Cyclosporine A-Independent Palmitate/Ca2+-Induced Permeability Transition Pore (PA-mPT Pore) and Its Role in Mitochondrial Function and Protection against Calcium Overload and Glutamate Toxicity

Mironova, G. D., & Pavlov, E. V. (2021) · Cells · doi:10.3390/cells10010125 · Cited by 29 · see citing works

Cold and freezing injury in insects: An overview of molecular mechanisms

Rozsypal, J. (2022) · European Journal of Entomology · doi:10.14411/eje.2022.005 · Cited by 25 · see citing works

A Novel Conceptual Model for the Dual Role of F O F 1 -ATP Synthase in Cell Life and Cell Death

Nath, S. (2020) · BioMolecular Concepts · doi:10.1515/bmc-2020-0014 · Cited by 24 · see citing works

Mitochondrial osmoregulation in evolution, cation transport and metabolism

Austin, S., & Nowikovsky, K. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2021.148368 · Cited by 21 · see citing works

Glutathione restores the mitochondrial redox status and improves the function of the cardiovascular system in old rats

Strutynska, N. A., Goshovska, Y. V., Mys, L. A., Strutynskyi, R. B., Luchkova, A. Y., Fedichkina, R. A., Okhai, I., Korkach, Y., & Sagach, V. F. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2022.1093388 · Cited by 20 · see citing works

How the mitochondrial calcium uniporter complex (MCU cx ) works

Boyman, L., & Lederer, W. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015886117 · Cited by 20 · see citing works

Methods of Measuring Mitochondrial Potassium Channels: A Critical Assessment

Walewska, A., Krajewska, M., Stefanowska, A., Buta, A., Bilewicz, R., Krysiński, P., Bednarczyk, P., Koprowski, P., & Szewczyk, A. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031210 · Cited by 20 · see citing works

The basics of mitochondrial cAMP signalling: Where, when, why

Benedetto, G. D., Lefkimmiatis, K., & Pozzan, T. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102320 · Cited by 20 · see citing works

High-fat diet activates liver iPLA2γ generating eicosanoids that mediate metabolic stress

Moon, S. H., Dilthey, B. G., Liu, X., Guan, S., Sims, H. F., & Gross, R. W. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100052 · Cited by 19 · see citing works

Recent Advances in the Characterization of Burkholderia Gladioli Pv. Cocovenenans and Its Toxin Production

Yuan, M., Han, R., Bai, L., Dong, Y., Xi, Q., Du, Q., Yang, Y., Forghani, F., Yang, Q., Ahn, J., et al. (2023) · Food Reviews International · doi:10.1080/87559129.2023.2199829 · Cited by 18 · see citing works

Incoming news on the F-type ATPase structure and functions in mammalian mitochondria

Nesci, S., & Pagliarani, A. (2020) · BBA Advances · doi:10.1016/j.bbadva.2020.100001 · Cited by 17 · see citing works

Cyclophilin D: Guardian or Executioner for Tumor Cells?

Zhang, L., Liu, Y., Zhou, R. L., He, B., Wang, W., & Zhang, B. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.939588 · Cited by 16 · see citing works

The ATPase Inhibitory Factor 1 is a Tissue-Specific Physiological Regulator of the Structure and Function of Mitochondrial ATP Synthase: A Closer Look Into Neuronal Function

Domínguez-Zorita, S., Romero-Carramiñana, I., Cuezva, J. M., & Esparza‐Moltó, P. B. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.868820 · Cited by 18 · see citing works

Amyloid β, α-synuclein and the c subunit of the ATP synthase: Can these peptides reveal an amyloidogenic pathway of the permeability transition pore?

Amodeo, G. F., & Pavlov, E. V. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183531 · Cited by 13 · see citing works

A ROS-responsive TPP-modified tanshinone IIA micelle improves DOX-induced heart failure

Zhao, Y. H., Wang, J., Zhang, Z., Kong, L., Liu, M., Chen, M., & Gao, L. (2025) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2025.125318 · Cited by 12 · see citing works

The Role of Autophagy in Excitotoxicity, Synaptic Mitochondrial Stress and Neurodegeneration

Chu, C. T. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2464376 · Cited by 12 · see citing works

Specific Features of Mitochondrial Dysfunction under Conditions of Ferroptosis Induced by t-Butylhydroperoxide and Iron: Protective Role of the Inhibitors of Lipid Peroxidation and Mitochondrial Permeability Transition Pore Opening

Федотчева, Т. А., Shimanovsky, N. L., & Fedotcheva, N. I. (2023) · Membranes · doi:10.3390/membranes13040372 · Cited by 11 · see citing works

ROMO1 overexpression protects the mitochondrial cysteinome from oxidations in aging

Xu, F., Huang, H., Peng, K., Jian, C., Wu, H., Jing, Z., Qiu, S., Chen, Y., Liu, K., Fu, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60503-z · Cited by 9 · see citing works

Involvement of Multidrug Resistance Modulators in the Regulation of the Mitochondrial Permeability Transition Pore

Федотчева, Т. А., Shimanovsky, N. L., & Fedotcheva, N. I. (2022) · Membranes · doi:10.3390/membranes12090890 · Cited by 9 · see citing works

BacFlash signals acid-resistance gene expression in bacteria

Wu, D., Qi, W., Nie, W., Lu, Z., Ye, A. Y., Li, J., Sun, T., Zhu, Y., Cheng, H., & Wang, X. (2020) · Cell Research · doi:10.1038/s41422-020-00431-3 · Cited by 9 · see citing works

Effects of Tl+ on the inner membrane thiol groups, respiration, and swelling in succinate-energized rat liver mitochondria were modified by thiol reagents

Korotkov, S. M. (2021) · BioMetals · doi:10.1007/s10534-021-00329-6 · Cited by 9 · see citing works

Maintained mitochondrial integrity without oxygen in the anoxia-tolerant crucian carp

Scott, M. A., Fagernes, C. E., Nilsson, G., & Stensløkken, K. (2024) · Journal of Experimental Biology · doi:10.1242/jeb.247409 · Cited by 8 · see citing works

Mitochondria Isolated from Hearts Subjected to Ischemia/Reperfusion Benefit from Adenine Nucleotide Translocase 1 Overexpression

Dörner, A., Lynetskiy, O., Euler, G., Landmesser, U., Schlüter, K., & Heger, J. (2021) · Membranes · doi:10.3390/membranes11110836 · Cited by 8 · see citing works

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 · see citing works

Mitochondrial quality control in health and disease: mechanisms and therapeutic targets

Creus, A., Mohapatra, S., Ortega, L., & Sebastián, D. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02813-2 · Cited by 7 · see citing works

Assessment of mitochondrial viability under calcium Stress: Insights for mitochondrial transplantation

Toosky, M., & Kheradvar, A. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102098 · Cited by 5 · see citing works

Influence of the Microbial Metabolite Acetyl Phosphate on Mitochondrial Functions Under Conditions of Exogenous Acetylation and Alkalization

Nv, B., & Fedotcheva, N. I. (2024) · Metabolites · doi:10.3390/metabo14120703 · Cited by 5 · see citing works

Studying Lipid-Related Pathophysiology Using the Yeast Model

Ralph-Epps, T., Onu, C., Vo, L., Schmidtke, M. W., Le, A., & Greenberg, M. L. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.768411 · Cited by 5 · see citing works

Glutathione Upregulates the Expression of KATP Channels and Vasorelaxation Responses and Inhibits mPTP Opening and Oxidative Stress in the Heart Mitochondria of Old Rats

Strutynskyi, R. B., Strutynska, N. A., Mys, L. A., Goshovska, Y. V., Korkach, Y., Fedichkina, R. A., Okhai, I., Strutynskyi, V. R., & Sagach, V. F. (2023) · BioMed Research International · doi:10.1155/2023/3562847 · Cited by 5 · see citing works

Potent Preorganized Pyrazolidine Cyclophilin D Inhibitors Prevent Mitochondrial and Organ Injury in a Mouse Pancreatitis Disease Model

Awais, M., Woodley, C. M., Guo, L., Rogers, M., Kershaw, N. M., Zacharchenko, T., Shore, E. R., Kattakayam, A., Mukherjee, R., Criddle, D. N., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01146 · Cited by 4 · see citing works

Cystic Fibrosis: Systems Biology Analysis from Homozygous p.Phe508del Variant Patients’ Samples Reveals Perturbations in Tissue‐Specific Pathways

Poloni, J. D. F., Rispoli, T., Rossetti, M. L. R., Trindade, C., & Vargas, J. E. (2021) · BioMed Research International · doi:10.1155/2021/5262000 · Cited by 4 · see citing works

The Mitochondrial Permeability Transition Pore Activates the Mitochondrial Unfolded Protein Response and Promotes AgingPreprint

Angeli, S., Foulger, A., Chamoli, M., Peiris, T. H., Gerencser, A. A., Shahmirzadi, A. A., Andersen, J. K., & Lithgow, G. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.03.366815 · Cited by 4 · see citing works

A splendid molecular factory: De- and reconstruction of the mammalian respiratory chain

Rimle, L., Phillips, B. P., Barra, I. M. C. C., Arnold, N., Hennebert, C., Meier, T. W., & von Ballmoos, C. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2416162122 · Cited by 3 · see citing works

Mitochondria for Cardiovascular Therapy: A Deep Dive into Drug Targets and Therapeutic Approaches

Semenzato, M., & Naón, D. (2025) · Current Pharmacology Reports · doi:10.1007/s40495-025-00405-2 · Cited by 3 · see citing works

Mitochondrial Transport Proteins in Cardiovascular Diseases: Metabolic Gatekeepers, Pathogenic Mediators and Therapeutic Targets

Pei, Y., Wan, S., Qi, J., Xi, X., Zhu, Y., An, P., Luo, J., & Luo, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178475 · Cited by 3 · see citing works

Disruption of ATP Synthase Spatiotemporal Organization, Ca 2+ Dynamics, and Contractile Function in Senescent Cardiomyocytes

Morris, S., Marx, N., Barrientos, G., Molina-Riquelme, I., Schmelter, F., Verdejo, H., Peischard, S., Seebohm, G., Eisner, V., & Busch, K. B. (2026) · Aging Cell · doi:10.1111/acel.70388 · Cited by 5 · see citing works

Looking Back to the Future of Mitochondrial Research

Bernardi, P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.682467 · Cited by 3 · see citing works

Editorial: Mitochondrial Exchangers and Transporters in Cell Survival and Death

Kwok, W.-M., Tajkhorshid, E., & Camara, A. K. S. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.745353 · Cited by 2 · see citing works

Unsolved mysteries and controversies of mitochondria in the heart – A virtual special issue in JMCC

Wang, W., & Sheu, S. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.04.022

Apoptosis en el corazón prediabético: Rol de la mitocondria y la comunicación retículo sarcoplasmático-mitocondria

Federico, M. (2021) · doi:10.35537/10915/115958

Unsolved mysteries and controversies of mitochondria in the heart – A virtual special issue in JMCC: Part IV

Wang, W., & Sheu, S. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.11.006

Cyclophilin D reduces Ca2+ sequestration by complement 1q binding protein

Adegbite, O. S., Adegbite, Y. I., Pickering, C., Criddle, D. N., & Lian, L. (2025) · Biochemical Journal · doi:10.1042/bcj20253361

Collapsin Response Mediator Protein 2 (CRMP2) Modulates Induction of the Mitochondrial Permeability Transition Pore in a Knock-In Mouse Model of Alzheimer’s Disease

Brustovetsky, T., Khanna, R., & Brustovetsky, N. (2026) · Cells · doi:10.3390/cells15020179

Redox Phenotyping of the Donor Heart: A New Paradigm for Precision Heart Transplantation

Urbanowicz, T. K., Kowalewski, M., Raffa, G. M., Krasińska, B., Pisano, C., Nuzzi, V., Rahnama, M., Suwalski, P., Krasiński, Z., & Grywalska, E. (2026) · Antioxidants · doi:10.3390/antiox15101261

The mitochondrial permeability transition pore: Molecular nature and role as a target in cardioprotection

Bernardi, P., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 499 · see citing works

The mitochondrial permeability transition: Recent progress and open questions

Bernardi, P., Carraro, M., & Lippe, G. (2021) · FEBS Journal · doi:10.1111/febs.16254 · Cited by 135 · see citing works

Mitochondrial Permeability Transition Pore Opening as a Promising Therapeutic Target in Cardiac Diseases

Javadov, S. A., Karmazyn, M., & Escobales, N. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.153213 · Cited by 248 · see citing works

The role of the mitochondrial permeability transition pore in heart disease

Halestrap, A. P., & Pasdois, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.017 · Cited by 362 · see citing works

From ATP to PTP and Back

Bernardi, P., Lisa, F. D., Fogolari, F., & Lippe, G. (2015) · Circulation Research · doi:10.1161/circresaha.115.306557 · Cited by 113 · see citing works