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

Molecular characterization of mitochondrial apoptosis-inducing factor

Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060

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

Keilin's Respiratory Chain Concept and Its Chemiosmotic Consequences

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

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

The mitochondrial uncoupling protein: structural and genetic studies.

Ricquier, D., & Bouillaud, F. (1997) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)61003-x · Cited by 52

The versatility and universality of calcium signalling

Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383

Mitochondria as sensors and regulators of calcium signalling

Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781

Calcium and ROS: A mutual interplay

Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546

The mitochondrial calcium uniporter is a highly selective ion channel

Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409

Biochemistry of exercise-induced metabolic acidosis

Robergs, R. A., Ghiasvand, F., & Parker, D. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00114.2004 · Cited by 1,304

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

A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis

Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072

Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines

Panov, A. V., Gutekunst, C.-A., Leavitt, B. R., Hayden, M. R., Burke, J. R., Strittmatter, W. J., & Greenamyre, J. T. (2002) · Nature Neuroscience · doi:10.1038/nn884 · Cited by 1,030

Drug-induced liver injury

Andrade, R. J., Chalasani, N., Björnsson, E. S., Suzuki, A., Kullak-Ublick, G. A., Watkins, P. B., Devarbhavi, H., Merz, M., Lucena, M. I., Kaplowitz, N., et al. (2019) · Nature Reviews Disease Primers · doi:10.1038/s41572-019-0105-0 · Cited by 924

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

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

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

Superoxide flashes in single mitochondria

Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.017 · Cited by 715

The permeability transition pore complex: another view

Halestrap, A. P., McStay, G. P., & Clarke, S. J. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01375-5 · Cited by 709

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

The mitochondrial permeability transition from in vitro 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

Control of aldosterone secretion: a model for convergence in cellular signaling pathways

SPÄT, A., & HUNYADY, L. (2004) · Physiological Reviews · doi:10.1152/physrev.00030.2003 · Cited by 494

Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function

Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471

Hepatocyte Death: A Clear and Present Danger

Malhi, H., Guicciardi, M. E., & Gores, G. J. (2010) · Physiological Reviews · doi:10.1152/physrev.00061.2009 · Cited by 477

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

The role of mitochondria in protection of the heart by preconditioning

Halestrap, A. P., Clarke, S. J., & Khaliulin, I. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.05.008 · Cited by 390

Role of Mitochondrial Inner Membrane Permeabilization in Necrotic Cell Death, Apoptosis, and Autophagy

Lemasters, J. J., Qian, T., He, L., Kim, J.-S., Elmore, S. P., Cascio, W. E., & Brenner, D. A. (2002) · Antioxidants & Redox Signaling · doi:10.1089/152308602760598918 · Cited by 377

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

Neuronal Calcium Homeostasis and Dysregulation

Gleichmann, M., & Mattson, M. P. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3386 · Cited by 360

Calcium signaling and exocytosis in adrenal chromaffin cells

García, A. G., García-De-Diego, A. M., Gandía, L., Borges, R., & García-Sancho, J. (2006) · Physiological Reviews · doi:10.1152/physrev.00039.2005 · Cited by 349

Increased longevity and refractoriness to Ca2+-dependent neurodegeneration in Surf1 knockout mice

Dell'Agnello, C., Leo, S., Agostino, A., Szabadkai, G., Tiveron, C., Zulian, A., Prelle, A., Roubertoux, P., Rizzuto, R., & Zeviani, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl477 · Cited by 308

A Mechanism of Virulence: Virulent Mycobacterium tuberculosis Strain H37Rv, but Not Attenuated H37Ra, Causes Significant Mitochondrial Inner Membrane Disruption in Macrophages Leading to Necrosis

Chen, M., Gan, H., & Remold, H. G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.6.3707 · Cited by 255

Mitochondria as Potential Targets in Alzheimer Disease Therapy: An Update

Cenini, G., & Voos, W. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00902 · Cited by 257

Identification of a dynamic mitochondrial protein complex driving cholesterol import, trafficking, and metabolism to steroid hormones

Rone, M. B., Midzak, A. S., Issop, L., Rammouz, G., Jagannathan, S., Fan, J., Ye, X., Blonder, J., Veenstra, T., & Papadopoulos, V. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1159 · Cited by 247

K channels and preconditioning: A re-examination of the role of mitochondrial K channels and an overview of alternative mechanisms

HANLEY, P., & DAUT, J. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.04.002 · Cited by 218

Mitochondrial functional specialization in glycolytic and oxidative muscle fibers: tailoring the organelle for optimal function

Picard, M., Hepple, R. T., & Burelle, Y. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00368.2011 · Cited by 214

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

The Involvement of Mg2+ in Regulation of Cellular and Mitochondrial Functions

Pilchova, I., Klacanova, K., Tatarkova, Z., Kaplan, P., & Racay, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6797460 · Cited by 198

Molecular Mechanisms for Bacterial Potassium Homeostasis

Stautz, J., Hellmich, Y., Fuss, M. F., Silberberg, J. M., Devlin, J. R., Stockbridge, R. B., & Hänelt, I. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166968 · Cited by 189

Mitochondrial bioenergetics in aging

Lenaz, G., D’Aurelio, M., Merlo Pich, M., Genova, M. L., Ventura, B., Bovina, C., Formiggini, G., & Parenti Castelli, G. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00177-8 · Cited by 189

Calcium Overload and Mitochondrial Metabolism

Walkon, L. L., Strubbe-Rivera, J. O., & Bazil, J. N. (2022) · Biomolecules · doi:10.3390/biom12121891 · Cited by 187

Cytochrome c Is Released from Mitochondria in a Reactive Oxygen Species (ROS)-dependent Fashion and Can Operate as a ROS Scavenger and as a Respiratory Substrate in Cerebellar Neurons Undergoing Excitotoxic Death

Atlante, A., Calissano, P., Bobba, A., Azzariti, A., Marra, E., & Passarella, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002361200 · Cited by 178

At the right distance: ER-mitochondria juxtaposition in cell life and death

Naon, D., & Scorrano, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.011 · Cited by 178

Human Na+/H+ exchanger isoform 6 is found in recycling endosomes of cells, not in mitochondria

Brett, C. L., Wei, Y., Donowitz, M., & Rao, R. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00420.2001 · Cited by 162

Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis

Tomasello, F., Messina, A., Lartigue, L., Schembri, L., Medina, C., Reina, S., Thoraval, D., Crouzet, M., Ichas, F., De Pinto, V., et al. (2009) · Cell Research · doi:10.1038/cr.2009.98 · Cited by 161

What is the function of mitochondrial networks? A theoretical assessment of hypotheses and proposal for future research

Hoitzing, H., Johnston, I. G., & Jones, N. S. (2015) · BioEssays · doi:10.1002/bies.201400188 · Cited by 159

Species- and tissue-specific relationships between mitochondrial permeability transition and generation of ROS in brain and liver mitochondria of rats and mice

Panov, A., Dikalov, S., Shalbuyeva, N., Hemendinger, R., Greenamyre, J. T., & Rosenfeld, J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00202.2006 · Cited by 141

Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition

DILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139

Interaction of peroxidized cardiolipin with rat‐heart mitochondrial membranes: Induction of permeability transition and cytochrome c release

Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137

The endogenous mitochondrial complex II inhibitor malonate regulates mitochondrial ATP-sensitive potassium channels: implications for ischemic preconditioning

Wojtovich, A. P., & Brookes, P. S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.025 · Cited by 119

Reduced reactive O2 species formation and preserved mitochondrial NADH and [Ca2+] levels during short-term 17 °C ischemia in intact hearts

Riess, M. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.09.016 · Cited by 118

Glutamate Transport Decreases Mitochondrial pH and Modulates Oxidative Metabolism in Astrocytes

Azarias, G., Perreten, H., Lengacher, S., Poburko, D., Demaurex, N., Magistretti, P. J., & Chatton, J.-Y. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4378-10.2011 · Cited by 107

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

Imeglimin prevents human endothelial cell death by inhibiting mitochondrial permeability transition without inhibiting mitochondrial respiration

Detaille, D., Vial, G., Borel, A.-L., Cottet-Rouselle, C., Hallakou-Bozec, S., Bolze, S., Fouqueray, P., & Fontaine, E. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.72 · Cited by 99

Voltage-dependant anion channels: novel insights into isoform function through genetic models

Raghavan, A., Sheiko, T., Graham, B. H., & Craigen, W. J. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.10.019 · Cited by 92

Mitochondrial dynamics: orchestrating the journey to advanced age

Biala, A. K., Dhingra, R., & Kirshenbaum, L. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.04.015 · Cited by 82

Gender modulation of Ca2+ uptake in cardiac mitochondria

ARIELI, Y. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.04.023 · Cited by 72

Exercise training induces respiratory substrate-specific decrease in Ca2+-induced permeability transition pore opening in heart mitochondria

Marcil, M., Bourduas, K., Ascah, A., & Burelle, Y. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00913.2005 · Cited by 71

The mitochondrial calcium regulator cyclophilin d is an essential component of oestrogen-mediated neuroprotection in amyotrophic lateral sclerosis

Kim, H. J., Magranè, J., Starkov, A. A., & Manfredi, G. (2012) · Brain · doi:10.1093/brain/aws208 · Cited by 64

Determination of the rate of K+ movement through potassium channels in isolated rat heart and liver mitochondria

Bednarczyk, P., Barker, G. D., & Halestrap, A. P. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.018 · Cited by 54

Ceramide Induces Release of Pro-Apoptotic Proteins from Mitochondria by Either a Ca2+-Dependent or a Ca2+-Independent Mechanism

Di Paola, M., Zaccagnino, P., Montedoro, G., Cocco, T., & Lorusso, M. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000023619.97392.0c · Cited by 52

The P66Shc/mitochondrial permeability transition pore pathway determines neurodegeneration

Savino, C., Pelicci, P., & Giorgio, M. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/719407 · Cited by 46

Decreased Susceptibility of Heart Mitochondria from Diabetic GK Rats to Mitochondrial Permeability Transition Induced by Calcium Phosphate

Oliveira, P. J., Rolo, A. P., Seiça, R., Palmeira, C. M., Santos, M. S., & Moreno, A. J. M. (2001) · Bioscience Reports · doi:10.1023/a:1010482017540 · Cited by 32

Dietary interventions designed to protect the perinatal brain from hypoxic-ischemic encephalopathy – Creatine prophylaxis and the need for multi-organ protection

Ellery, S. J., Dickinson, H., McKenzie, M., & Walker, D. W. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2015.11.002 · Cited by 23

Mitochondrial Ultrastructure and Glucose Signaling Pathways Attributed to the Kv1.3 Ion Channel

Kovach, C. P., Al Koborssy, D., Huang, Z., Chelette, B. M., Fadool, J. M., & Fadool, D. A. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00178 · Cited by 20

Structure and function of the human mitochondrial MRS2 channel

(2024) · doi:10.1038/s41594-024-01420-5 · Cited by 17