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

Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+

Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works

Mitochondrial membrane permeabilization in cell death

Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works

Mitochondria and cell death: outer membrane permeabilization and beyond

Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · see citing works

The mitochondrial permeability transition pore and its role in cell death

CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432 · 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

A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology

Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · see citing works

Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells

Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938 · see citing works

The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis

Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · 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

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

Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,534 · see citing works

Mitochondria

Newmeyer, D. D., & Ferguson-Miller, S. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00116-8 · Cited by 1,268 · see citing works

Mitochondria and calcium: from cell signalling to cell death

Duchen, M. R. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00057.x · Cited by 1,261 · 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

Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971 · see citing works

STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1

Park, C. Y., Hoover, P., Mullins, F. M., Bachhawat, P., Covington, E. D., Raunser, S., Walz, T., García, K. C., Dolmetsch, R. E., & Lewis, R. S. (2009) · Cell · doi:10.1016/j.cell.2009.02.014 · Cited by 947 · 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

VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis

Cheng, E. H.-Y., Sheiko, T. V., Fisher, J. K., Craigen, W. J., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1083995 · Cited by 852 · 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

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

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

p53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis

Vaseva, A. V., Marchenko, N. D., Ji, K., Tsirka, S. E., Holzmann, S., & Moll, U. M. (2012) · Cell · doi:10.1016/j.cell.2012.05.014 · Cited by 740 · see citing works

Solution structure of the integral human membrane protein VDAC-1 in detergent micelles

Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G. (2008) · Science · doi:10.1126/science.1161302 · Cited by 667 · see citing works

MICU1 Is an Essential Gatekeeper for MCU-Mediated Mitochondrial Ca2+ Uptake that Regulates Cell Survival

Mallilankaraman, K. B., Doonan, P. J., Cárdenas, C., Chandramoorthy, H. C. K., Müller, M., Miller, R., Hoffman, N. E., Gandhirajan, R. K., Molgó, J., Birnbaum, M. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.011 · Cited by 661 · 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

Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor

Hung, Y. P., Albeck, J. G., Tantama, M., & Yellen, G. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.012 · Cited by 509 · see citing works

MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism

Mallilankaraman, K. B., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C. K., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2622 · Cited by 487 · 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

Erratum: Corrigenda: MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism

Mallilankaraman, K. B., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C. K., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3202 · Cited by 418 · see citing works

The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria

Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., & Langer, T. (2005) · Cell · doi:10.1016/j.cell.2005.08.003 · Cited by 398 · 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

Mitochondrial calcium uptake

Williams, G. S. B., Boyman, L., Chikando, A. C., Khairallah, R. J., & Lederer, W. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300410110 · Cited by 362 · see citing works

Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport

Ferreirinha, F., Quattrini, A., Pirozzi, M., Valsecchi, V., Dina, G., Broccoli, V., Auricchio, A., Piemonte, F., Tozzi, G., Gaeta, L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420138 · Cited by 308 · 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

VDAC structure, selectivity, and dynamics

Colombini, M. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.026 · Cited by 274 · see citing works

MCUR1は細胞代謝を制御するミトコンドリアCa 2MCUR1+ 取込の必須成分である

Mallilankaraman, K. B., Cesar, C., Patrick, J., Harish, C. C., Krishna, M. I., Golenár, T., Gyoergy, C., Madireddi, P., Jun, Y., Müller, M., et al. (2012) · Nature Cell Biology · Cited by 270 · see citing works

Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport

Ferreirinha, F., Quattrini, A., Pirozzi, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20138 · Cited by 264 · see citing works

Variable and Tissue-Specific Subunit Composition of Mitochondrial m-AAA Protease Complexes Linked to Hereditary Spastic Paraplegia

Koppen, M., Metodiev, M. D., Casari, G., Rugarli, E. I., & Langer, T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01470-06 · Cited by 203 · see citing works

The Role of Mitochondrial Porins and the Permeability Transition Pore in Learning and Synaptic Plasticity

Weeber, E. J., Levy, M., Sampson, M. J., Anflous, K., Armstrong, D. L., Brown, S. E., Sweatt, J. D., & Craigen, W. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201649200 · Cited by 181 · see citing works

Involvement of Cyclophilin D in the Activation of A mitochondrial Pore by Ca2+ and Oxidant Stress

Tanveer, A., Virji, S., Andreeva, L. V., Totty, N. F., Hsuan, J. J., Ward, J. M., & Crompton, M. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0166q.x · Cited by 166 · see citing works

MICU1 Motifs Define Mitochondrial Calcium Uniporter Binding and Activity

Hoffman, N. E., Chandramoorthy, H. C. K., Shanmughapriya, S., Zhang, X., Rajan, S., Mallilankaraman, K. B., Gandhirajan, R. K., Vagnozzi, R. J., Ferrer, L. M., Sreekrishnanilayam, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.11.026 · Cited by 138 · see citing works

Altered Mitochondrial Sensitivity for ADP and Maintenance of Creatine-stimulated Respiration in Oxidative Striated Muscles from VDAC1-deficient Mice

Anflous, K., Armstrong, D. D., & Craigen, W. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006587200 · Cited by 132 · see citing works

Ca 2+ signals regulate mitochondrial metabolism by stimulating CREB-mediated expression of the mitochondrial Ca 2+ uniporter gene MCU

Shanmughapriya, S., Rajan, S., Hoffman, N. E., Zhang, X., Guo, S., Kolesar, J. E., Hines, K. J., Ragheb, J. G., Jog, N. R., Caricchio, R., et al. (2015) · Science Signaling · doi:10.1126/scisignal.2005673 · Cited by 123 · see citing works

MitoMiner: a data warehouse for mitochondrial proteomics data

Smith, A. C., Blackshaw, J., & Robinson, A. J. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1101 · Cited by 90 · see citing works

Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia

Rugarli, E. I., & Langer, T. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.04.002 · Cited by 76 · see citing works

Mitochondrial calcium handling and oxidative stress

Halestrap, A. P., Griffiths, E. J., & Connern, C. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210353 · Cited by 72 · see citing works

Relationships between Ca2+ release, Ca2+ cycling, and Ca2+-mediated permeability changes in mitochondria.

Riley, W. W., & Pfeiffer, D. R. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38890-7 · Cited by 65 · see citing works

Enhancement of anxiety, facilitation of avoidance behavior, and occurrence of adult-onset obesity in mice lacking mitochondrial cyclophilin D

Luvisetto, S., Basso, E., Petronilli, V., Bernardi, P., & Forte, M. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.030 · Cited by 59 · see citing works

Mitochondrial calcium in health and disease

Halestrap, A. P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.07.011 · Cited by 40 · see citing works

The role of Cyclophilin D in learning and memory

Mouri, A., Noda, Y., Shimizu, S., Tsujimoto, Y., & Nabeshima, T. (2009) · Hippocampus · doi:10.1002/hipo.20625 · Cited by 21 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Neuronal Cell Death

Fricker, M., Tolkovsky, A. M., Borutaitė, V., Coleman, M. P., & Brown, G. C. (2018) · Physiological Reviews · doi:10.1152/physrev.00011.2017 · Cited by 1,122 · see citing works

Molecular mechanisms and consequences of mitochondrial permeability transition

Bonora, M., Giorgi, C., & Pinton, P. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00433-y · Cited by 549 · see citing works

Mitochondria, Bioenergetics and Apoptosis in Cancer

Burke, P. J. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.10.006 · Cited by 431 · see citing works

Cytosolic escape of mitochondrial DNA triggers cGAS-STING-NLRP3 axis-dependent nucleus pulposus cell pyroptosis

Zhang, W., Li, G., Luo, R., Lei, J., Song, Y., Wang, B., Ma, L., Liao, Z., Ke, W., Liu, H., et al. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00729-9 · Cited by 329 · see citing works

Mitochondrial permeability transition pore is a potential drug target for neurodegeneration

Rao, V. K., Carlson, E. A., & Yan, S. S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.003 · Cited by 325 · see citing works

Hereditary spastic paraplegia: from diagnosis to emerging therapeutic approaches

Shribman, S., Reid, E., Crosby, A. H., Houlden, H., & Warner, T. T. (2019) · The Lancet Neurology · doi:10.1016/s1474-4422(19)30235-2 · Cited by 304 · see citing works

Calcium Dynamics as a Machine for Decoding Signals

Giorgi, C., Danese, A., Missiroli, S., Patergnani, S., & Pinton, P. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.01.002 · Cited by 282 · see citing works

Mitochondrial Ca2+ Uniporter Is a Mitochondrial Luminal Redox Sensor that Augments MCU Channel Activity

Dong, Z., Shanmughapriya, S., Tomar, D., Siddiqui, N., Lynch, S., Nemani, N., Breves, S. L., Zhang, X., Tripathi, A., Palaniappan, P., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.032 · Cited by 233 · see citing works

Mitochondrial Permeability Uncouples Elevated Autophagy and Lifespan Extension

Zhou, B., Kreuzer, J., Kumsta, C., Wu, L., Kamer, K. J., Cedillo, L., Zhang, Y., Li, S., Kacergis, M. C., Webster, C. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.013 · Cited by 220 · 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

MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics

Tomar, D., Dong, Z., Shanmughapriya, S., Koch, D. A., Thomas, T. P., Hoffman, N. E., Timbalia, S. A., Goldman, S. J., Breves, S. L., Corbally, D. P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.050 · Cited by 210 · see citing works

Mitochondrial Permeability Transition: New Findings and Persisting Uncertainties

Izzo, V., Bravo-San Pedro, J. M., Sica, V., Kroemer, G., & Galluzzi, L. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.04.006 · Cited by 205 · 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

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

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

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

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

Mutations in <i>VPS13D</i> lead to a new recessive ataxia with spasticity and mitochondrial defects

Seong, E., Insolera, R., Dulovic, M., Kamsteeg, E., Trinh, J., Brüggemann, N., Sandford, E., Li, S., Ozel, A. B., Li, J. Z., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25220 · Cited by 163 · see citing works

A Selective and Cell-Permeable Mitochondrial Calcium Uniporter (MCU) Inhibitor Preserves Mitochondrial Bioenergetics after Hypoxia/Reoxygenation Injury

Woods, J. J., Nemani, N., Shanmughapriya, S., Kumar, A., Zhang, M., Nathan, S. R., Thomas, M., Carvalho, E. J., Karthik, R., Srikantan, S., et al. (2019) · ACS Central Science · doi:10.1021/acscentsci.8b00773 · Cited by 161 · see citing works

VDAC1 functions in Ca2+ homeostasis and cell life and death in health and disease

Shoshan‐Barmatz, V., Krelin, Y., & Shteinfer‐Kuzmine, A. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.06.007 · Cited by 162 · see citing works

Mitochondrial permeability transition pore: Sensitivity to opening and mechanistic dependence on substrate availability

Briston, T., Roberts, M., Lewis, S., Powney, B., M. Staddon, J., Szabadkai, G., & Duchen, M. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-10673-8 · Cited by 152 · see citing works

Mitochondrial Ca2+ Transport: Mechanisms, Molecular Structures, and Role in Cells

Belosludtsev, K. N., Dubinin, M. V., Belosludtseva, N. V., & Mironova, G. D. (2019) · Biochemistry (Moscow) · doi:10.1134/s0006297919060026 · Cited by 142 · see citing works

Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition

Vercesi, A. E., Castilho, R. F., Kowaltowski, A. J., Oliveira, H. C. F., de Souza-Pinto, N. C., Figueira, T. R., & Busanello, E. N. B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.034 · Cited by 141 · see citing works

Physiopathology of the Permeability Transition Pore: Molecular Mechanisms in Human Pathology

Bonora, M., Patergnani, S., Ramaccini, D., Morciano, G., Pedriali, G., Kahsay, A., Bouhamida, E., Giorgi, C., Wieckowski, M., & Pinton, P. (2020) · Biomolecules · doi:10.3390/biom10070998 · Cited by 135 · see citing works

m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration

Patrón, M., Sprenger, H., & Langer, T. (2018) · Cell Research · doi:10.1038/cr.2018.17 · Cited by 134 · see citing works

The mitochondrial permeability transition pore in AD 2016: An update

Biasutto, L., Azzolini, M., Szabó, I., & Zoratti, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.02.012 · Cited by 128 · see citing works

The Classification of Autosomal Recessive Cerebellar Ataxias: a Consensus Statement from the Society for Research on the Cerebellum and Ataxias Task Force

Beaudin, M., Matilla‐Dueñas, A., Soong, B., Pedroso, J. L., Barsottini, O. G. P., Mitoma, H., Tsuji, S., Schmahmann, J. D., Manto, M. U., Rouleau, G. A., et al. (2019) · The Cerebellum · doi:10.1007/s12311-019-01052-2 · Cited by 128 · 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

Melatonin and mitochondrial function during ischemia/reperfusion injury

Ma, Z., Xin, Z., Di, W., Yan, X., Li, X., Reiter, R. J., & Yang, Y. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2618-6 · Cited by 124 · see citing works

The Mitochondrial Voltage-Dependent Anion Channel 1, Ca2+ Transport, Apoptosis, and Their Regulation

Shoshan‐Barmatz, V., De, S., & Meir, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00060 · Cited by 122 · see citing works

Diabetes Mellitus, Mitochondrial Dysfunction and Ca2+-Dependent Permeability Transition Pore

Belosludtsev, K. N., Belosludtseva, N. V., & Dubinin, M. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186559 · Cited by 122 · see citing works

Regulation of necrotic cell death: p53, PARP1 and cyclophilin D-overlapping pathways of regulated necrosis?

Yuan, Y., & Padanilam, B. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2202-5 · Cited by 119 · see citing works

Mitochondrial permeability transition pore: a potential drug target for neurodegeneration

Kalani, K., Yan, S. F., & Yan, S. S. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.08.001 · Cited by 117 · see citing works

Cyclophilin D, Somehow a Master Regulator of Mitochondrial Function

Porter, G. A., & Beutner, G. (2018) · Biomolecules · doi:10.3390/biom8040176 · Cited by 114 · see citing works

MIRO-1 Determines Mitochondrial Shape Transition upon GPCR Activation and Ca2+ Stress

Nemani, N., Carvalho, E., Tomar, D., Dong, Z., Ketschek, A., Breves, S. L., Jaña, F., Worth, A. M., Heffler, J., Palaniappan, P., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.098 · Cited by 111 · see citing works

Prohibitin 1 regulates mtDNA release and downstream inflammatory responses

Liu, H., Fan, H., He, P., Zhuang, H., Liu, X., Chen, M., Zhong, W., Zhang, Y., Zhen, C., Li, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022111173 · Cited by 106 · see citing works

Mitochondrial calcium cycling in neuronal function and neurodegeneration

Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105 · see citing works

The Role of Mitochondria in Liver Ischemia‐Reperfusion Injury: From Aspects of Mitochondrial Oxidative Stress, Mitochondrial Fission, Mitochondrial Membrane Permeable Transport Pore Formation, Mitophagy, and Mitochondria‐Related Protective Measures

Zhang, H., Yan, Q., Wang, X., Chen, X., Chen, Y., Du, J., & Chen, L. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6670579 · Cited by 104 · see citing works

Double-activation of mitochondrial permeability transition pore opening via calcium overload and reactive oxygen species for cancer therapy

Zhou, Y., Jing, S., Liu, S., Shen, X., Cai, L., Zhu, C., Zhao, Y., & Pang, M. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01392-y · Cited by 104 · see citing works

Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium threshold for the mitochondrial permeability transition

Chaudhuri, D., Artiga, D. J., Abiria, S. A., & Clapham, D. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602264113 · Cited by 102 · see citing works

Blockade of MCU-Mediated Ca2+ Uptake Perturbs Lipid Metabolism via PP4-Dependent AMPK Dephosphorylation

Tomar, D., Jaña, F., Dong, Z., Quinn, W. J., Jadiya, P., Breves, S. L., Daw, C. C., Srikantan, S., Shanmughapriya, S., Nemani, N., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.107 · Cited by 95 · see citing works

Mitochondrial permeability transition in cardiac ischemia–reperfusion: whether cyclophilin D is a viable target for cardioprotection?

Javadov, S. A., Jang, S., Parodi‐Rullán, R. M., Khuchua, Z. A., & Kuznetsov, A. V. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2502-4 · Cited by 97 · see citing works

Mitochondria-Associated Proteostasis

Ruan, L., Wang, Y., Zhang, X., Tomaszewski, A., McNamara, J. T., & Li, R. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-121219-081604 · Cited by 95 · 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

Mitochondrial MPTP: A Novel Target of Ethnomedicine for Stroke Treatment by Apoptosis Inhibition

Li, Y., Sun, J., Wu, R., Bai, J., Hou, Y., Zeng, Y., Zhang, Y., Wang, X., Wang, Z., & Meng, X. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00352 · Cited by 91 · see citing works

Insights into Clinical, Genetic, and Pathological Aspects of Hereditary Spastic Paraplegias: A Comprehensive Overview

Elsayed, L. E. O., Eltazi, I., Ahmed, A. E., & Stévanin, G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.690899 · Cited by 90 · see citing works

Anion Channels of Mitochondria

Ponnalagu, D., & Singh, H. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_39 · Cited by 87 · see citing works

Mitochondria in endothelial cells angiogenesis and function: current understanding and future perspectives

Luo, Z., Yao, J., Wang, Z., & Xu, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04286-1 · Cited by 87 · see citing works

The Dual Function of Reactive Oxygen/Nitrogen Species in Bioenergetics and Cell Death: The Role of ATP Synthase

Kaludercic, N., & Giorgio, V. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3869610 · Cited by 88 · see citing works

Small-Molecule Inhibitors of Cyclophilins Block Opening of the Mitochondrial Permeability Transition Pore and Protect Mice From Hepatic Ischemia/Reperfusion Injury

Panel, M., Ruiz, I., Brillet, R., Lafdil, F., Teixeira-Clerc, F., Nguyễn, C. T., Caldéraro, J., Gelin, M., Allemand, F., Guichou, J., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.07.026 · Cited by 83 · see citing works

Mitochondrial Dysfunction in Age‐Related Metabolic Disorders

Natarajan, V., Chawla, R., Mah, T. K. L., Vivekanandan, R., Tan, S., Sato, P. Y., & Mallilankaraman, K. B. (2020) · PROTEOMICS · doi:10.1002/pmic.201800404 · Cited by 81 · see citing works

SARS-CoV-2 infection enhances mitochondrial PTP complex activity to perturb cardiac energetics

Karthik, R., Maity, S., Muthukumar, A. R., Kandala, S., Tomar, D., El‐Aziz, T. M. A., Allen, C., Sun, Y., Venkatesan, M., Madaris, T. R., et al. (2022) · iScience · doi:10.1016/j.isci.2021.103722 · Cited by 72 · see citing works

Mitochondrial pyruvate and fatty acid flux modulate MICU1-dependent control of MCU activity

Nemani, N., Dong, Z., Daw, C. C., Madaris, T. R., Karthik, R., Enslow, B. T., Rubannelsonkumar, C. S., Shanmughapriya, S., Mallireddigari, V., Maity, S., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aaz6206 · Cited by 71 · see citing works

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

Carraro, M., Carrer, A., Urbani, A., & Bernardi, P. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.05.014 · Cited by 71 · see citing works

The still uncertain identity of the channel-forming unit(s) of the mitochondrial permeability transition pore

Baines, C. P., & Gutiérrez‐Aguilar, M. (2018) · Cell Calcium · doi:10.1016/j.ceca.2018.05.003 · Cited by 70 · see citing works

Ion Channels in Plant Bioenergetic Organelles, Chloroplasts and Mitochondria: From Molecular Identification to Function

Carraretto, L., Teardo, E., Checchetto, V., Finazzi, G., Uozumi, N., & Szabó, I. (2016) · Molecular Plant · doi:10.1016/j.molp.2015.12.004 · Cited by 68 · see citing works

The mitochondrial permeability transition pore in Ca2+ homeostasis

Carraro, M., & Bernardi, P. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102719 · Cited by 64 · see citing works

Mitochondrial disorders and the eye

Kisilevsky, E., Freund, P. R., & Margolin, E. (2019) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2019.11.001 · Cited by 63 · see citing works

Parkinsonism and spastic paraplegia type 7: Expanding the spectrum of mitochondrial Parkinsonism

la Casa‐Fages, B. D., Fernández‐Eulate, G., Gámez, J., Barahona‐Hernando, R., Morís, G., García‐Barcina, M., Infante, J., Zulaica, M., Fernández‐Pelayo, U., Muñoz‐Oreja, M., et al. (2019) · Movement Disorders · doi:10.1002/mds.27812 · Cited by 63 · see citing works

The short variant of optic atrophy 1 (OPA1) improves cell survival under oxidative stress

Lee, H., Smith, S. B., Sheu, S., & Yoon, Y. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010983 · Cited by 63 · see citing works

Cross-link assisted spatial proteomics to map sub-organelle proteomes and membrane protein topologies

Zhu, Y., Akkaya, K. C., Ruta, J., Yokoyama, N., Wang, C., Ruwolt, M., Lima, D. B., Lehmann, M., & Liu, F. (2024) · Nature Communications · doi:10.1038/s41467-024-47569-x · Cited by 62 · see citing works

The Mitochondrial Permeability Transition Pore and ATP Synthase

Beutner, G., Alavian, K. N., Jonas, E. A., & Porter, G. A. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_5 · Cited by 61 · see citing works

MFF Regulation of Mitochondrial Cell Death Is a Therapeutic Target in Cancer

Seo, J. H., Chae, Y. C., Kossenkov, A. V., Lee, Y. G., Tang, H., Agarwal, E., Gabrilovich, D. I., Languino, L. R., Speicher, D. W., Shastrula, P. K., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1982 · Cited by 61 · see citing works

Astrocytic metabolic switch is a novel etiology for Cocaine and HIV-1 Tat-mediated neurotoxicity

Natarajaseenivasan, K., Cotto, B., Shanmughapriya, S., Lombardi, A. A., Datta, P. K., Madesh, M., Elrod, J. W., Khalili, K., & Langford, D. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0422-3 · Cited by 60 · see citing works

Mitochondrial functions and rare diseases

Dard, L., Blanchard, W., Hubert, C., Lacombe, D., & Rossignol, R. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100842 · Cited by 61 · see citing works

Ca2+-mediated mitochondrial inner membrane permeabilization induces cell death independently of Bax and Bak

Quarato, G., Llambi, F., Guy, C. S., Min, J., Actis, M., Sun, H., Narina, S., Pruett‐Miller, S. M., Peng, J., Ranković, Z., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01025-9 · Cited by 70 · see citing works

Mitochondrial permeability transition pore: Back to the drawing board

Chinopoulos, C. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.010 · Cited by 55 · see citing works

VDAC and its interacting partners in plant and animal systems: an overview

Kanwar, P., Samtani, H., Sanyal, S. K., Srivastava, A. K., Suprasanna, P., & Pandey, G. K. (2020) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2020.1756214 · Cited by 56 · see citing works

Mitochondria focused neurotherapeutics for spinal cord injury

Rabchevsky, A. G., Michael, F. M., & Patel, S. P. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113332 · Cited by 56 · see citing works

Impaired flickering of the permeability transition pore causes SPG7 spastic paraplegia

Sambri, I., Massa, F., Gullo, F., Meneghini, S., Cassina, L., Carraro, M., Dina, G., Quattrini, A., Patanella, L., Carissimo, A., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.103050 · Cited by 54 · 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

Recent progress in the use of mitochondrial membrane permeability transition pore in mitochondrial dysfunction-related disease therapies

Cui, Y., Pan, M., Ma, J., Song, X., Cao, W., & Zhang, P. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03926-0 · Cited by 53 · see citing works

Regulation of Cell Death by Mitochondrial Transport Systems of Calcium and Bcl-2 Proteins

Naumova, N., & Šachl, R. (2020) · Membranes · doi:10.3390/membranes10100299 · Cited by 51 · see citing works

Inorganic polyphosphate (polyP) as an activator and structural component of the mitochondrial permeability transition pore

Solesio, M. E., Elustondo, P. A., Zakharian, E., & Pavlov, E. V. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150206 · Cited by 50 · see citing works

Impact of intracellular ion channels on cancer development and progression

Peruzzo, R., Biasutto, L., Szabó, I., & Leanza, L. (2016) · European Biophysics Journal · doi:10.1007/s00249-016-1143-0 · Cited by 49 · see citing works

Targeting the mitochondrial permeability transition pore for drug discovery: Challenges and opportunities

Boyenle, I. D., Oyedele, A.-Q. K., Ogunlana, A. T., Adeyemo, A. F., Oyelere, S. F., Akinola, O. B., Adelusi, T. I., Ehigie, L. O., & Ehigie, A. F. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.01.006 · Cited by 48 · see citing works

Redox proteome analysis of auranofin exposed ovarian cancer cells (A2780)

Chiappetta, G., Gamberi, T., Faienza, F., Limaj, X., Rizza, S., Luigi Messori, A., Filomeni, G., Modesti, A., & Vinh, J. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102294 · Cited by 47 · see citing works

Long COVID-19 and the Heart: Is Cardiac Mitochondria the Missing Link?

Chang, X., Ismail, N. I., Rahman, A., Xu, D., Chan, R. W. Y., Ong, S., & Ong, S. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0126 · Cited by 50 · see citing works

A Novel In Vitro CypD-Mediated p53 Aggregation Assay Suggests a Model for Mitochondrial Permeability Transition by Chaperone Systems

Lebedev, I., Nemajerová, A., Foda, Z. H., Kornaj, M., Tong, M., Moll, U. M., & Seeliger, M. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.001 · Cited by 47 · see citing works

Mitochondrial calcium signalling and neurodegenerative diseases

Britti, E., Delaspre, F., Tamarit, J., & Ros, J. (2018) · Neuronal Signaling · doi:10.1042/ns20180061 · Cited by 47 · see citing works

Approaches to monitor ATP levels in living cells: where do we stand?

Ley‐Ngardigal, S., & Bertolin, G. (2021) · FEBS Journal · doi:10.1111/febs.16169 · Cited by 45 · see citing works

Regulation of mitochondrial bioenergetics by the non-canonical roles of mitochondrial dynamics proteins in the heart

Wang, W., Fernández‐Sanz, C., & Sheu, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.004 · Cited by 45 · see citing works

Mitochondrial Quality Control Strategies: Potential Therapeutic Targets for Neurodegenerative Diseases?

Hu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44 · see citing works

Glucosylceramide accumulation in microglia triggers STING-dependent neuroinflammation and neurodegeneration in mice

Wang, R., Sun, H., Cao, Y., Zhang, Z., Chen, Y., Wang, X., Liu, L., Wu, J., Xu, H., Wu, D., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adk8249 · Cited by 44 · see citing works

Permeabilization of the outer mitochondrial membrane: Mechanisms and consequences

Yapryntseva, M. A., Zhivotovsky, B., & Gogvadze, V. G. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167317 · Cited by 44 · see citing works

Quantification of active mitochondrial permeability transition pores using GNX-4975 inhibitor titrations provides insights into molecular identity

Richardson, A. P., & Halestrap, A. P. (2016) · Biochemical Journal · doi:10.1042/bcj20160070 · Cited by 42 · see citing works

Molecular Biomarkers of the Mitochondrial Quality Control Are Differently Affected by Hypoxia-Reoxygenation Stress in Marine Bivalves Crassostrea gigas and Mytilus edulis

Steffen, J. B. M., Falfushynska, H., Piontkivska, H., & Sokolova, I. M. (2020) · Frontiers in Marine Science · doi:10.3389/fmars.2020.604411 · Cited by 43 · see citing works

Chemical Modulation of Mitochondria–Endoplasmic Reticulum Contact Sites

Rebelo, A. P. M., Bello, F. D., Knedlík, T., Kaar, N., Volpin, F., Shin, S. H., & Giacomello, M. (2020) · Cells · doi:10.3390/cells9071637 · Cited by 41 · see citing works

Mitochondrial Dysfunction in Genetic and Non-Genetic Parkinson’s Disease

Lucchesi, M., Biso, L., Bonaso, M., Longoni, B., Buchignani, B., Battini, R., Santorelli, F. M., Doccini, S., & Scarselli, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094451 · Cited by 39 · see citing works

Forty years later: Mitochondria as therapeutic targets in muscle diseases

Zulian, A., Schiavone, M., Giorgio, V., & Bernardi, P. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.043 · Cited by 37 · see citing works

Loss of Mitochondrial AAA Proteases AFG3L2 and YME1L Impairs Mitochondrial Structure and Respiratory Chain Biogenesis

Cesnekova, J., Rodinová, M., Hansíková, H., Zeman, J., & Stibůrek, L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123930 · Cited by 35 · see citing works

Consequences of inner mitochondrial membrane protein misfolding

Coyne, L. P., & Chen, X. J. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.001 · Cited by 34 · 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

Nicotinamide adenine dinucleotide emerges as a therapeutic target in aging and ischemic conditions

Hosseini, L., Vafaee, M. S., Mahmoudi, J., & Badalzadeh, R. (2019) · Biogerontology · doi:10.1007/s10522-019-09805-6 · Cited by 36 · see citing works

Mitochondrial F-ATP Synthase and Its Transition into an Energy-Dissipating Molecular Machine

Lippe, G., Coluccino, G., Zancani, M., Baratta, W., & Crusiz, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8743257 · Cited by 36 · see citing works

The Mitochondrial Calcium Uniporter Interacts with Subunit c of the ATP Synthase of Trypanosomes and Humans

Huang, G., & Docampo, R. (2020) · mBio · doi:10.1128/mbio.00268-20 · Cited by 35 · see citing works

NIPSNAP protein family emerges as a sensor of mitochondrial health

Fathi, E., Yarbro, J. M., & Homayouni, R. (2021) · BioEssays · doi:10.1002/bies.202100014 · Cited by 33 · see citing works

Roles of Specialized Pro-Resolving Lipid Mediators in Cerebral Ischemia Reperfusion Injury

Yin, P., Wei, Y., Wang, X., Zhu, M., & Feng, J. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00617 · Cited by 33 · see citing works

Altered mitochondrial calcium handling and cell death by necroptosis: An emerging paradigm

Faizan, M. I., & Ahmad, T. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.004 · Cited by 31 · see citing works

Commentary: SPG7 is an essential and conserved component of the mitochondrial permeability transition pore

Bernardi, P., & Forte, M. A. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00320 · Cited by 27 · see citing works

Genetic manipulation of SPG7 or NipSnap2 does not affect mitochondrial permeability transition

Klutho, P. J., Dashek, R. J., Song, L., & Baines, C. P. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-0239-6 · Cited by 11 · 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

Genetic Dissection of the Permeability Transition Pore

Forte, M. A., & Bernardi, P. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6565-9 · Cited by 79 · see citing works

The Mitochondrial Permeability Transition Pore

Morganti, C., Bonora, M., Sbano, L., Morciano, G., Aquila, G., Campo, G. C., Wieckowski, M. R., Giorgi, C., & Pinton, P. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_5 · Cited by 12 · see citing works