The mitochondrial permeability transition from in vitro artifact to disease target

Bernardi, Paolo; Krauskopf, Alexandra; Basso, Emy; Petronilli, Valeria; Blalchy‐Dyson, Elizabeth; Di Lisa, Fabio; Forte, Michael A.

doi:10.1111/j.1742-4658.2006.05213.x

Cited by 627Mitochondrial Function and PathologyCell death mechanisms and regulationCardiac Ischemia and Reperfusion

The DOI matches its Crossref record; 276 of the 276 references it cites were found in a registry or an index.

The mitochondrial permeability transition from in vitro artifact to disease target

Bernardi, Paolo, Krauskopf, Alexandra, Basso, Emy, Petronilli, Valeria, Blalchy‐Dyson, Elizabeth, Di Lisa, Fabio, Forte, Michael A.·2006·The FEBS Journal

DOI 10.1111/j.1742-4658.2006.05213.x

Open this paper in CoChat — free account

Abstract

The mitochondrial permeability transition pore is a high conductance channel whose opening leads to an increase of mitochondrial inner membrane permeability to solutes with molecular masses up to approximately 1500 Da. In this review we trace the rise of the permeability transition pore from the status of in vitro artifact to that of effector mechanism of cell death. We then cover recent results based on genetic inactivation of putative permeability transition pore components, and discuss their meaning for our understanding of pore structure. Finally, we discuss evidence indicating that the permeability transition pore plays a role in pathophysiology, with specific emphasis on in vivo models of disease.

Integrity signals

Registry

Crossref · 10.1111/j.1742-4658.2006.05213.x

Cites

276 of 276 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Since these dysfunctions are known to activate mPTP, mPTP activity is expected to be enhanced in dysfunctional mitochondria in aging.
“Since these dysfunctions are known to activate mPTP [2], it can be expected that mPTP activity will be enhanced in dysfunctional mitochondria in aging.”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [2]

Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
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
Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,487
Homozygous Defect in HIV-1 Coreceptor Accounts for Resistance of Some Multiply-Exposed Individuals to HIV-1 Infection
Liu, R., Paxton, W. A., Choe, S., Ceradini, D., Martin, S. R., Horuk, R., MacDonald, M. E., Stuhlmann, H., Koup, R. A., & Landau, N. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80110-5 · Cited by 3,074
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins
Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., & Vaux, D. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00009-x · Cited by 2,372
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
Endonuclease G is an apoptotic DNase when released from mitochondria
Li, L. Y., Luo, X., & Wang, X. (2001) · Nature · doi:10.1038/35083620 · Cited by 1,787
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
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
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
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Self-citation
The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy
Lemasters, J. J., Nieminen, A.-L., Qian, T., Trost, L. C., Elmore, S. P., Nishimura, Y., Crowe, R. A., Cascio, W. E., Bradham, C. A., Brenner, D. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00112-1 · Cited by 1,387
Mitochondrial permeability transition pore opening during myocardial reperfusion—a target for cardioprotection
Halestrap, A. P. (2003) · Cardiovascular Research · doi:10.1016/s0008-6363(03)00533-9 · Cited by 1,244
Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis
Giorgio, M., Migliaccio, E., Orsini, F., Paolucci, D., Moroni, M., Contursi, C., Pelliccia, G., Luzi, L., Minucci, S., Marcaccio, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.011 · Cited by 1,176
Self-citation
Bcl-2 inhibits the mitochondrial release of an apoptogenic protease.
Susín, S. A., Zamzami, N., Castedo, M., Hirsch, T., Marchetti, P., Macho, A., Daugas, É., Geuskens, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1331 · Cited by 1,133
Ca 2+ -Induced Apoptosis Through Calcineurin Dephosphorylation of BAD
Wang, H., Pathan, N., Ethell, I. M., Krajewski, S., Yamaguchi, Y., Shibasaki, F., McKeon, F., Bobo, T., Franke, T. F., & Reed, J. C. (1999) · Science · doi:10.1126/science.284.5412.339 · Cited by 1,132
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
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
Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
Zhu, S., Stavrovskaya, I. G., Drozda, M., Kim, B. Y. S., Ona, V. O., Li, M., Sarang, S. S., Liu, A. S., Hartley, D. M., Wu, D. C., et al. (2002) · Nature · doi:10.1038/417074a · Cited by 1,069
The mitochondrion in apoptosis: how Pandora's box opens
Zamzami, N., & Kroemer, G. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35048073 · Cited by 1,055
Glycogen synthase kinase-3β mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore
Juhaszova, M., Zorov, D. B., Kim, S.-H., Pepe, S., Fu, Q., Fishbein, K. W., Ziman, B. D., Wang, S., Ytrehus, K., Antos, C. L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19906 · Cited by 1,041
The internal structure of mitochondria
Frey, T., & Mannella, C. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01609-1 · Cited by 949
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 872
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
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
Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
Griffiths, E. J., & Halestrap, A. P. (1995) · Biochemical Journal · doi:10.1042/bj3070093 · Cited by 838
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
Apoptotic Pathways: Ten Minutes to Dead
Green, D. R. (2005) · Cell · doi:10.1016/j.cell.2005.05.019 · Cited by 826
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
Self-citation
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
Mitochondria and cell death
Bernardi, P., Scorrano, L., Colonna, R., Petronilli, V., & Lisa, F. D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00725.x · Cited by 757
Self-citation
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
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 748
Identification of Omi/HtrA2 as a Mitochondrial Apoptotic Serine Protease That Disrupts Inhibitor of Apoptosis Protein-Caspase Interaction
Hegde, R. P., Srinivasula, S. M., Zhang, Z., Wassell, R. P., Mukattash, R., Cilenti, L., DuBois, G. C., Lazebnik, Y. A., Zervos, A. S., Fernandes‐Alnemri, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109721200 · Cited by 745
Keilin's Respiratory Chain Concept and Its Chemiosmotic Consequences
Mitchell, P. (1979) · Science · doi:10.1126/science.388618 · Cited by 738
Mitochondrial Binding of Hexokinase II Inhibits Bax-induced Cytochrome c Release and Apoptosis
Pastorino, J. G., Shulga, N., & Hoek, J. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109950200 · Cited by 720
Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier
McEnery, M. W., Snowman, A. M., Trifiletti, R. R., & Snyder, S. H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.8.3170 · Cited by 708
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
Mitochondrial calcium transport: physiological and pathological relevance
Gunter, T. E., Gunter, K. K., Sheu, S. S., & Gavin, C. E. (1994) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1994.267.2.c313 · Cited by 698
The peripheral-type benzodiazepine receptor. Localization to the mitochondrial outer membrane.
Anholt, R. R. H., Pedersen, P. L., Souza, E. B. D., & Snyder, S. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36131-8 · Cited by 696
The Permeability Transition Pore Complex: A Target for Apoptosis Regulation by Caspases and Bcl-2–related Proteins
Marzo, I., Brenner, C., Zamzami, N., Susín, S. A., Beutner, G., Brdiczka, D. G., Rémy, R., Xie, Z.-H., Reed, J. C., & Kroemer, G. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.8.1261 · Cited by 684
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
Self-citation
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
Self-citation
Hexokinase-Mitochondria Interaction Mediated by Akt Is Required to Inhibit Apoptosis in the Presence or Absence of Bax and Bak
Majewski, N., Nogueira, V., Bhaskar, P. T., Coy, P. E., Skeen, J. E., Gottlob, K., Chandel, N. S., Thompson, C. B., Robey, R. B., & Hay, N. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.014 · Cited by 638
Relationship between configuration, function, and permeability in calcium-treated mitochondria.
Hunter, D. R., Haworth, R. A., & Southard, J. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33220-9 · Cited by 619
Role of the Mitochondrial Permeability Transition in Myocardial Disease
Weiss, J. N., Kôrge, P., Honda, H. M., & Ping, P. (2003) · Circulation Research · doi:10.1161/01.res.0000087542.26971.d4 · Cited by 610
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
Inhibiting mitochondrial permeability transition pore opening: a new paradigm for myocardial preconditioning?
Hausenloy, D. J. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00455-8 · Cited by 585
Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
Bernardi, P., Broekemeier, K. M., & Pfeiffer, D. R. (1994) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762735 · Cited by 561
Self-citation
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
Alcohol and mitochondria: a dysfunctional relationship
Hoek, J. B., Cahill, A., & Pastorino, J. G. (2002) · Gastroenterology · doi:10.1053/gast.2002.33613 · Cited by 553
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 533
Self-citation
Modulation of the Mitochondrial Permeability Transition Pore by Pyridine Nucleotides and Dithiol Oxidation at Two Separate Sites
Costantini, P., Chernyak, B. V., Petronilli, V., & Bernardi, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6746 · Cited by 516
Self-citation
Poly (ADP-ribose) polymerase, nitric oxide and cell death
Pieper, A. A. (1999) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(99)01292-4 · Cited by 512
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
Self-citation
The Adenine Nucleotide Translocase: A Central Component of the Mitochondrial Permeability Transition Pore and Key Player in Cell Death
Halestrap, A. P., & Brenner, C. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457278 · Cited by 505
MITOCHONDRIAL CALCIUM OVERLOAD: A GENERAL MECHANISM FOR CELL-NECROSIS IN MUSCLE DISEASES
Wrogemann, K., & Pena, S. (1976) · The Lancet · doi:10.1016/s0140-6736(76)92781-1 · Cited by 500
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
Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
Halestrap, A. P., Kerr, P. M., Javadov, S. A., & Woodfield, K. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00122-4 · Cited by 485
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
Self-citation
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
Self-citation
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 466
Self-citation
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 463
Self-citation
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
Protein Kinase Cε Interacts With and Inhibits the Permeability Transition Pore in Cardiac Mitochondria
Baines, C. P., Song, C., Zheng, Y.-T., Wang, G.-W., Zhang, J., Wang, O.-L., Guo, Y., Bolli, R., Cardwell, E. M., & Ping, P. (2003) · Circulation Research · doi:10.1161/01.res.0000069215.36389.8d · Cited by 454
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
Self-citation
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 438
A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis
Trinei, M., Giorgio, M., Cicalese, A., Barozzi, S., Ventura, A., Migliaccio, E., Milia, E., Padura, I. M., Raker, V. A., Maccarana, M., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205513 · Cited by 436
Self-citation
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
A mitochondrial perspective on cell death
Bernardi, P., Petronilli, V., Lisa, F. D., & Forte, M. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01745-x · Cited by 418
Self-citation
In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death
AZOULAY-ZOHAR, H., ISRAELSON, A., ABU-HAMAD, S., & SHOSHAN-BARMATZ, V. (2004) · Biochemical Journal · doi:10.1042/bj20031465 · Cited by 408
Activation of Glycogen Synthase Kinase 3β Disrupts the Binding of Hexokinase II to Mitochondria by Phosphorylating Voltage-Dependent Anion Channel and Potentiates Chemotherapy-Induced Cytotoxicity
Pastorino, J. G., Hoek, J. B., & Shulga, N. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1925 · Cited by 405
Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function
GINCEL, D., ZAID, H., & SHOSHAN-BARMATZ, V. (2001) · Biochemical Journal · doi:10.1042/bj3580147 · Cited by 396
Mitochondrial permeability transition in CNS trauma: Cause or effect of neuronal cell death?
Sullivan, P. G., Rabchevsky, A. G., Waldmeier, P. C., & Springer, J. E. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20292 · Cited by 387
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
Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis
Papadopoulos, V., Amri, H., Boujrad, N., Cascio, C., Culty, M., Garnier, M., Hardwick, M., Li, H., Vidic, B., Brown, A. S., et al. (1997) · Steroids · doi:10.1016/s0039-128x(96)00154-7 · Cited by 386
Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide
Nieminen, A. L., Saylor, A. K., Tesfai, S. A., Herman, B. A., & Lemasters, J. J. (1995) · Biochemical Journal · doi:10.1042/bj3070099 · Cited by 381
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
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
Cyclosporin A, But Not FK 506, Protects Mitochondria and Neurons against Hypoglycemic Damage and Implicates the Mitochondrial Permeability Transition in Cell Death
Friberg, H., Ferrand-Drake, M., Bengtsson, F., Halestrap, A. P., & Wieloch, T. W. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-14-05151.1998 · Cited by 366
Specific inhibition of the mitochondrial permeability transition prevents lethal reperfusion injury
Argaud, L., Gateau-Roesch, O., Muntean, D. M., Chalabreysse, L., Loufouat, J., Robert, D., & Ovize, M. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.12.001 · Cited by 359
Regulation of the Permeability Transition Pore in Skeletal Muscle Mitochondria
Fontaine, E. M., Eriksson, O., Ichas, F., & Bernardi, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12662 · Cited by 358
Self-citation
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
Evidence for the presence of a reversible Ca2+-dependent pore activated by oxidative stress in heart mitochondria
Crompton, M., COSTI, A., & Hayat, L. (1987) · Biochemical Journal · doi:10.1042/bj2450915 · Cited by 345
Peripheral benzodiazepine binding sites: Effect of PK 11195, 1-(2-chlorophenyl)-n-methyl-n-(1-methylpropyl)-3-isoquinolinecarboxamide
Fur, G. L., Perrier, M. L., Vaucher, N., Imbault, F., Flamier, A., Bénavidès, J., Uzan, A., Renault, C., Dubroeucq, M. C., & Gueremy, C. (1983) · Life Sciences · doi:10.1016/0024-3205(83)90062-0 · Cited by 345
Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
Beutner, G., Rück, A., Riede, B., & Brdiczka, D. G. (1998) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00175-2 · Cited by 342
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
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
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
Self-citation
Involvement of mitochondrial permeability transition in acetaminophen-induced liver injury in mice
Masubuchi, Y., Suda, C., & Horie, T. (2004) · Journal of Hepatology · doi:10.1016/j.jhep.2004.09.015 · Cited by 317
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
Collagen VI deficiency induces early onset myopathy in the mouse: an animal model for Bethlem myopathy
Bonaldo, P. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.13.2135 · Cited by 306
Porphyrins are endogenous ligands for the mitochondrial (peripheral-type) benzodiazepine receptor.
Verma, A. M., Nye, J. S., & Snyder, S. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2256 · Cited by 301
Kinetic evidence for a heart mitochondrial pore activated by Ca 2+ , inorganic phosphate and oxidative stress
Crompton, M., & COSTI, A. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14475.x · Cited by 299
Poly(ADP-ribose) polymerase: killer or conspirator? The ‘suicide hypothesis’ revisited
Chiarugi, A. (2002) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01902-7 · Cited by 298
Ullrich scleroatonic muscular dystrophy is caused by recessive mutations in collagen type VI
Vanegas, O. C., Bertini, E., Zhang, R.-Z., Petrini, S., Minosse, C., Sabatelli, P., Giusti, B., Chu, M.-L., & Pepe, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121027598 · Cited by 298
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
Arachidonic Acid Causes Cell Death through the Mitochondrial Permeability Transition
Scorrano, L., Penzo, D., Petronilli, V., Pagano, F. C., & Bernardi, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010603200 · Cited by 294
Self-citation
Cyclosporin and carnitine prevent the anoxic death of cultured hepatocytes by inhibiting the mitochondrial permeability transition
Pastorino, J. G., Snyder, J. W., Serroni, A., Hoek, J. B., & Farber, J. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85172-4 · Cited by 292
The relationship between mitochondrial membrane permeability, membrane potential, and the retention of Ca2+ by mitochondria.
Beatrice, M. C., Palmer, J. W., & Pfeiffer, D. R. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43551-x · Cited by 291
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
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
THE EFFECT OF THYROXINE AND OTHER SUBSTANCES ON THE SWELLING OF ISOLATED RAT LIVER MITOCHONDRIA
Tapley, D. F. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50798-0 · Cited by 279
Endotoxin-induced mitochondrial damage correlates with impaired respiratory activity
Crouser, E. D., JULIAN, M. W., Blaho, D. V., & Pfeiffer, D. R. (2002) · Critical Care Medicine · doi:10.1097/00003246-200202000-00002 · Cited by 277
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
Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A
Nazareth, W. (1991) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(91)90181-k · Cited by 272
Imaging the Permeability Pore Transition in Single Mitochondria
Hüser, J., Rechenmacher, C. E., & Blatter, L. A. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77920-2 · Cited by 269
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
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
Peripheral-Type Benzodiazepine Receptors in Endocrine Organs: Autoradiographic Localization in Rat Pituitary, Adrenal, and Testis*
Souza, E. B. D., Anholt, R. R. H., MURPHY, K. M. M., Snyder, S. H., & Kuhar, M. J. (1985) · Endocrinology · doi:10.1210/endo-116-2-567 · Cited by 266
An Intrathecal Bolus of Cyclosporin a before Injury Preserves Mitochondrial Integrity and Attenuates Axonal Disruption in Traumatic Brain Injury
Okonkwo, D. O., & Povlishock, J. T. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199904000-00010 · Cited by 263
Hexokinase II: The Integration of Energy Metabolism and Control of Apoptosis
Pastorino, J. G., & Hoek, J. B. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457269 · Cited by 257
PK11195, a Ligand of the Mitochondrial Benzodiazepine Receptor, Facilitates the Induction of Apoptosis and Reverses Bcl-2-Mediated Cytoprotection
Hirsch, T., Decaudin, D., Susín, S. A., Marchetti, P., Larochette, N., Resche-Rigon, M., & Kroemer, G. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4084 · Cited by 254
Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures
Jöbsis, G. J., Ijlst‐Keizers, H., Vreijling, J. P., de Visser, M., Speer, M. C., Wolterman, R. A., Baas, F., & Bolhuis, P. A. (1996) · Nature Genetics · doi:10.1038/ng0996-113 · Cited by 248
Immotile Sperm and Infertility in Mice Lacking Mitochondrial Voltage-dependent Anion Channel Type 3
Sampson, M. J., Decker, W. K., Beaudet, A. L., Ruitenbeek, W., Armstrong, D. L., Hicks, J. M., & Craigen, W. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104724200 · Cited by 247
Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
Connern, C. P., & Halestrap, A. P. (1994) · Biochemical Journal · doi:10.1042/bj3020321 · Cited by 246
A pore way to die
Halestrap, A. P. (2005) · Nature · doi:10.1038/434578a · Cited by 245
Patch-clamping of the inner mitochondrial membrane reveals a voltage-dependent ion channel
Sorgato, M. C., Keller, B. U., & Stühmer, W. (1987) · Nature · doi:10.1038/330498a0 · Cited by 245
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
Self-citation
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
Self-citation
Mitochondrial structure and function in acute myocardial ischemic injury.
Jennings, R. B., & Ganote, C. E. (1976) · PubMed · Cited by 232
Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore. II. The minimal requirements for pore induction underscore a key role for transmembrane electrical potential, matrix pH, and matrix Ca2+.
Petronilli, V., Cola, C., & Bernardi, P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54034-5 · Cited by 228
Self-citation
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
Peripheral benzodiazepine binding sites: Effect of PK 11195, 1-(2-chlorophenyl)-n-methyl-(1-methylpropyl)-3 isoquinolinecarboxamide
Fur, G. L., Guilloux, F., Rufat, P., Bénavidès, J., Uzan, A., Renault, C., Dubroeucq, M. C., & Gueremy, C. (1983) · Life Sciences · doi:10.1016/0024-3205(83)90063-2 · Cited by 227
Cyclosporin A Significantly Ameliorates Cortical Damage Following Experimental Traumatic Brain Injury in Rodents
Scheff, S. W., & Sullivan, P. G. (1999) · Journal of Neurotrauma · doi:10.1089/neu.1999.16.783 · Cited by 227
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
Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
Zalk, R., Israelson, A., GARTY, E. S., Azoulay‐Zohar, H., & Shoshan‐Barmatz, V. (2005) · Biochemical Journal · doi:10.1042/bj20041356 · Cited by 226
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
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
Further evidence that cyclosporin A protects mitochondria from calcium overload by inhibiting a matrix peptidyl-prolyl cis-trans isomerase. Implications for the immunosuppressive and toxic effects of cyclosporin
Griffiths, E. J., & Halestrap, A. P. (1991) · Biochemical Journal · doi:10.1042/bj2740611 · Cited by 220
Blockade of the Mitochondrial Permeability Transition Pore Diminishes Infarct Size in the Rat after Transient Middle Cerebral Artery Occlusion
Matsumoto, S., Friberg, H., Ferrand-Drake, M., & Wieloch, T. W. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199907000-00002 · Cited by 215
Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
Zheng, Y., Shi, Y., Tian, C., Jiang, C., Jin, H., Chen, J., Almasan, A., Tang, H., & Chen, Q. (2003) · Oncogene · doi:10.1038/sj.onc.1207205 · Cited by 206
NADH regulates the gating of VDAC, the mitochondrial outer membrane channel.
Zizi, M., Forte, M. A., Blachly‐Dyson, E., & Colombini, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42070-9 · Cited by 205
Self-citation
Mitochondrial permeability transitions: how many doors to the house?
Zoratti, M., Szabó, I., & Marchi, U. D. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.10.006 · Cited by 205
Mitochondrial benzodiazepine receptor linked to inner membrane ion channels by nanomolar actions of ligands.
Kinnally, K. W., Zorov, D. B., Antonenko, Y. N., Snyder, S. H., McEnery, M. W., & Tedeschi, H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1374 · Cited by 205
Mitochondrial autophagy and injury in the liver in α 1 -antitrypsin deficiency
Teckman, J. H., An, J.-K., Blomenkamp, K., Schmidt, B. Z., & Perlmutter, D. H. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00175.2003 · Cited by 201
Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes.
Bernardi, P., & AZZONE, G. F. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68946-5 · Cited by 199
Self-citation
Mitochondrial permeability transition in the switch from necrotic to apoptotic cell death in ischemic rat hepatocytes
Kim, J. (2003) · Gastroenterology · doi:10.1053/gast.2003.50059 · Cited by 198
Cyclosporin A limits calcium-induced axonal damage following traumatic brain injury
Okonkwo, D. O., Büki, A., Siman, R. G., & Povlishock, J. T. (1999) · Neuroreport · doi:10.1097/00001756-199902050-00026 · Cited by 198
Event timing turns punishment to reward
Tanimoto, H., Heisenberg, M., & Gerber, B. (2004) · Nature · doi:10.1038/430983a · Cited by 197
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 196
Self-citation
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
Continuous Infusion of Cyclosporin A Postinjury Significantly Ameliorates Cortical Damage Following Traumatic Brain Injury
Sullivan, P. G., Thompson, M., & Scheff, S. W. (2000) · Experimental Neurology · doi:10.1006/exnr.1999.7282 · Cited by 192
Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
Connern, C. P., & Halestrap, A. P. (1992) · Biochemical Journal · doi:10.1042/bj2840381 · Cited by 191
Amelioration by cyclosporin A of brain damage in transient forebrain ischemia in the rat
Uchino, H., Elmér, E., Uchino, K., Li, P.-A., He, Q., Smith, M., & Siesjö, B. K. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00902-0 · Cited by 186
Mitochondrial function as a determinant of recovery or death in cell response to injury
Lisa, F. D., & Bernardi, P. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_25 · Cited by 184
Self-citation
Role of mitochondrial permeability transition in diclofenac-induced hepatocyte injury in rats
Masubuchi, Y., Nakayama, S., & Horie, T. (2002) · Hepatology · doi:10.1053/jhep.2002.31871 · Cited by 184
Mouse VDAC Isoforms Expressed in Yeast: Channel Properties and Their Roles in Mitochondrial Outer Membrane Permeability
Xu, X. (1999) · The Journal of Membrane Biology · doi:10.1007/s002329900540 · Cited by 182
Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization
Lin, D.-T., & Lechleiter, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112035200 · Cited by 181
The mitochondrial permeability transition pore may comprise VDAC molecules
Szabó, I., Pinto, V. D., & Zoratti, M. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80274-x · Cited by 178
The reversible Ca2+-induced permeabilization of rat liver mitochondria
Al-Nasser, I., & Crompton, M. (1986) · Biochemical Journal · doi:10.1042/bj2390019 · Cited by 175
A heart mitochondrial Ca2+-dependent pore of possible relevance to re-perfusion-induced injury. Evidence that ADP facilitates pore interconversion between the closed and open states
Crompton, M., & COSTI, A. (1990) · Biochemical Journal · doi:10.1042/bj2660033 · Cited by 173
Arachidonic Acid Released by Phospholipase A2 Activation Triggers Ca2+-dependent Apoptosis through the Mitochondrial Pathway
Penzo, D., Petronilli, V., Angelin, A., Cusan, C., Colonna, R., Scorrano, L., Pagano, F. C., Prato, M., Lisa, F. D., & Bernardi, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310381200 · Cited by 166
Self-citation
Pathophysiological relevance of mitochondria in NAD+ metabolism
Lisa, F. D., & Ziegler, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02198-6 · Cited by 161
VDAC Channels
Blachly‐Dyson, E., & Forte, M. A. (2001) · IUBMB Life · doi:10.1080/15216540152845902 · Cited by 159
Self-citation
Structural and Functional Study of Reconstituted Peripheral Benzodiazepine Receptor
Lacapère, J.-J., Delavoie, F., Li, H., Péranzi, G., Maccario, J., Papadopoulos, V., & Vidić, B. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4975 · Cited by 156
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
Mitochondrial function as a determinant of recovery or death in cell response to injury
Lisa, F. D., & Bernardi, P. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006810523586 · Cited by 150
Self-citation
Rotenone Inhibits the Mitochondrial Permeability Transition-induced Cell Death in U937 and KB Cells
Chauvin, C., Oliveira, F. D., Ronot, X., Mousseau, M., Leverve, X. M., & Fontaine, E. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106417200 · Cited by 147
Electrophysiology of the inner mitochondrial membrane
Zoratti, M., & Szab�, I. (1994) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762739 · Cited by 146
Posttreatment with the immunosuppressant cyclosporin A in transient focal ischemia
Yoshimoto, T., & Siesjö, B. K. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01733-3 · Cited by 143
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
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
Self-citation
Critical role of ASK1 in the 6‐hydroxydopamine‐induced apoptosis in human neuroblastoma SH‐SY5Y cells
Ouyang, M., & Shen, X. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03730.x · Cited by 139
Opening of the mitochondrial permeability transition pore causes matrix expansion and outer membrane rupture in fas-mediated hepatic apoptosis in mice
Feldmann, G., Haouzi, D., Moreau, A., Durand‐Schneider, A., Bringuier, A. F., Berson, A., Mansouri, A., Fau, D., & Pessayre, D. (2000) · Hepatology · doi:10.1002/hep.510310318 · Cited by 138
Protection by acidotic pH against anoxia/reoxygenation injury to rat neonatal cardiac myocytes
Bond, J. M., Herman, B. A., & Lemasters, J. J. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91887-i · Cited by 137
Properties of a Cyclosporin-insensitive Permeability Transition Pore in Yeast Mitochondria
Jung, D. W., Bradshaw, P. C., & Pfeiffer, D. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21104 · Cited by 137
Intracellular pH and Ca2+ homeostasis in the pH paradox of reperfusion injury to neonatal rat cardiac myocytes
Bond, J. M., Chacon, E., Herman, B. A., et al. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.265.1.c129 · Cited by 136
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 135
Protoporphyrin IX, an endogenous ligand of the peripheral benzodiazepine receptor, potentiates induction of the mitochondrial permeability transition and the killing of cultured hepatocytes by rotenone.
Pastorino, J. G., Simbula, G., Gilfor, E., Hoek, J. B., & Farber, J. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47387-5 · Cited by 132
The Mechanism of Neuroprotection by Topiramate in an Animal Model of Epilepsy
Kudin, A. P., Dębska–Vielhaber, G., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Epilepsia · doi:10.1111/j.0013-9580.2004.13504.x · Cited by 132
Cyclosporin A Improves Brain Tissue Oxygen Consumption and Learning/Memory Performance after Lateral Fluid Percussion Injury in Rats
Alessandri, B., Rice, A. C., Levasseur, J. E., DeFord, M., Hamm, R. J., & Bullock, M. R. (2002) · Journal of Neurotrauma · doi:10.1089/08977150260190429 · Cited by 129
The role of mitochondria in the salvage and the injury of the ischemic myocardium
Lisa, F. D., Menabò, R., Canton, M., & Petronilli, V. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00121-2 · Cited by 126
Self-citation
Calcium and pyridine nucleotide interaction in mitochondrial membranes
Vinogradov, A., Scarpa, A., & Chance, B. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90261-5 · Cited by 126
Dual role for the ADP/ATP translocator?
Halestrap, A. P. (2004) · Nature · doi:10.1038/nature02816 · Cited by 124
Peripheral Benzodiazepine Receptor Agonists Exhibit Potent Antiapoptotic Activities
Bono, F., Lamarche, I., Prabonnaud, V., Fur, G. L., & Herbert, J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1683 · Cited by 122
Toxicity of Alpidem, a Peripheral Benzodiazepine Receptor Ligand, but Not Zolpidem, in Rat Hepatocytes: Role of Mitochondrial Permeability Transition and Metabolic Activation
Berson, A., Descatoire, V., Sutton, A., Fau, D., Maulny, B., Vadrot, N., Feldmann, G., BERTHON, B., Tordjmann, T., & Pessayre, D. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29292-2 · Cited by 118
Peripheral-type benzodiazepine receptor ligands:
Chelli, B., Falleni, A., Salvetti, F., Gremigni, V., Lucacchini, A., & Martini, C. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00588-8 · Cited by 115
Amelioration by cyclosporin A of brain damage following 5 or 10 min of ischemia in rats subjected to preischemic hyperglycemia
Li, P.-A., Uchino, H., Elmér, E., & Siesjö, B. K. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00005-x · Cited by 114
Intrathecal cyclosporin prolongs survival of late-stage ALS mice
Keep, M. F., Elmér, E., Fong, K. S. K., & Csiszár, K. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02012-1 · Cited by 114
The powerhouse takes control of the cell: Is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death?
Stavrovskaya, I. G., & Kristal, B. S. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.032 · Cited by 113
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 110
Self-citation
Peripheral-type benzodiazepine receptor (PBR) and PBR drug ligands in fibroblast and fibrosarcoma cell proliferation: role of ERK, c-Jun and ligand-activated PBR-independent pathways
Kletsas, D., Li, W., Han, Z. J., & Papadopoulos, V. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.01.021 · Cited by 107
The presence of two classes of high‐affinity cyclosporin A binding sites in mitochondria
McGuinness, O. M., YAFEI, N., COSTI, A., & Crompton, M. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15667.x · Cited by 105
Mitochondria and reperfusion injury
Lisa, F. D., Canton, M., Menabò, R., Dodoni, G., & Bernardi, P. (2003) · Basic Research in Cardiology · doi:10.1007/s00395-003-0415-x · Cited by 105
Self-citation
Mitochondrial control of neuron death and its role in neurodegenerative disorders
Jordán, J., Ceña, V., & Prehn, J. H. M. (2003) · Journal of Physiology and Biochemistry · doi:10.1007/bf03179878 · Cited by 104
Ammonia Neurotoxicity: Role of the Mitochondrial Permeability Transition
Rao, K. V. R., Jayakumar, A. R., & Norenberg, M. D. (2003) · Metabolic Brain Disease · doi:10.1023/a:1023858902184 · Cited by 102
Mitochondria and aging: A role for the permeability transition?
Crompton, M. (2004) · Aging Cell · doi:10.1046/j.1474-9728.2003.00073.x · Cited by 101
Fluoxetine (Prozac) interaction with the mitochondrial voltage‐dependent anion channel and protection against apoptotic cell death
Nahon, E., Israelson, A., Abu-Hamad, S., & Shoshan-Barmatz, V. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.020 · Cited by 101
Ro5-4864, a peripheral benzodiazepine receptor ligand, reduces reactive gliosis and protects hippocampal hilar neurons from kainic acid excitotoxicity
Veiga, S., Azcoitia, I., & Garcia-Segura, L. M. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20430 · Cited by 101
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
Growth and senescence of Medicago truncatula cultured cells are associated with characteristic mitochondrial morphology
Zottini, M., Barizza, E., Bastianelli, F., et al. (2006) · New Phytologist · doi:10.1111/j.1469-8137.2006.01830.x · Cited by 98
Cyclosporin A protects hepatocytes subjected to high Ca2+ and oxidative stress
Broekemeier, K. M., Carpenter-Deyo, L. J., Reed, D. J., & Pfeiffer, D. R. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80616-o · Cited by 95
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
Regulation of the Mitochondrial Permeability Transition Pore by Ubiquinone Analogs. A Progress Report
Walter, L., Miyoshi, H., Leverve, X. M., Bernardi, P., & Fontaine, E. M. (2002) · Free Radical Research · doi:10.1080/10715760290021252 · Cited by 94
Self-citation
Acidosis Promotes the Permeability Transition in Energized Mitochondria: Implications for Reperfusion Injury
Kristián, T., Bernardi, P., & Siesjö, B. K. (2001) · Journal of Neurotrauma · doi:10.1089/08977150152693755 · Cited by 91
Self-citation
Oxygen-induced enzyme release after irreversible myocardial injury. Effects of cyanide in perfused rat hearts.
Ganote, C. E., Worstell, J., & Kaltenbach, J. P. (1976) · PubMed Central · Cited by 88

Flagged first, then by citations

Research works printed but not linked: 5

Raaflaub J, 1953, Die schwellung isolierter leberzell mitochondrien und ihre physikalisch beeinfluβarkeit, Helv Physiol Pharmacol Acta, 11, 142
Raaflaub J, 1953, Über den wirkungsmechanismus von adenosintriphosphat (ATP) als cofaktor isolierter mitochondrien, Helv Physiol Pharmacol Acta, 11, 157
Brenner‐Holzach O, 1954, Die korrelation zwischen der schwellung isolierter mitochondrien und dem abbau intramitochondrialen adenosinnucleotide (ATP, ADP, AMP, CoA), Helv Physiol Pharmacol Acta, 12, 242
10.1042/0264-6021:3580147 · DOI · Paper page
10.1016/S0014-5793(01)03314-2 · DOI

Sorted by citations

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
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215
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
Oxidized DNA fragments exit mitochondria via mPTP- and VDAC-dependent channels to activate NLRP3 inflammasome and interferon signaling
Xian, H., Watari, K., Sanchez-Lopez, E., Offenberger, J., Onyuru, J., Sampath, H., Ying, W., Hoffman, H. M., Shadel, G. S., & Karin, M. (2022) · Immunity · doi:10.1016/j.immuni.2022.06.007 · Cited by 850
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654
Autophagy is defective in collagen VI muscular dystrophies, and its reactivation rescues myofiber degeneration
Grumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540
Self-citation
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
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
Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore
Leung, A. W. C., & Halestrap, A. P. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.009 · Cited by 323
The path from mitochondrial ROS to aging runs through the mitochondrial permeability transition pore
Rottenberg, H., & Hoek, J. B. (2017) · Aging Cell · doi:10.1111/acel.12650 · Cited by 275
Tnf induces pathogenic programmed macrophage necrosis in tuberculosis through a mitochondrial-lysosomal-endoplasmic reticulum circuit
Roca, F. J., Whitworth, L. J., Redmond, S., Jones, A. A., & Ramakrishnan, L. (2019) · Cell · doi:10.1016/j.cell.2019.08.004 · Cited by 233
Spare respiratory capacity, oxidative stress and excitotoxicity
Nicholls, D. G. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371385 · Cited by 161
Mitochondrially targeted effects of berberine [Natural Yellow 18, 5,6-dihydro-9,10-dimethoxybenzo(g)-1,3-benzodioxolo(5,6-a) quinolizinium] on K1735-M2 mouse melanoma cells: comparison with direct effects on isolated mitochondrial fractions
Pereira, G. C., Branco, A. F., Matos, J. A. C., Pereira, S. L., Parke, D., Perkins, E. L., Serafim, T. L., Sardão, V. A., Santos, M. S., Moreno, A. J. M., et al. (2007) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.128017 · Cited by 152
The mitochondria-targeted anti-oxidant MitoQ decreases ischemia-reperfusion injury in a murine syngeneic heart transplant model
Dare, A. J., Logan, A., Prime, T. A., Rogatti, S., Goddard, M., Bolton, E. M., Bradley, J. A., Pettigrew, G. J., Murphy, M. P., & Saeb-Parsy, K. (2015) · The Journal of Heart and Lung Transplantation · doi:10.1016/j.healun.2015.05.007 · Cited by 119
Forward operation of adenine nucleotide translocase during F 0 F 1 ‐ATPase reversal: critical role of matrix substrate‐level phosphorylation
Chinopoulos, C., Gerencser, A. A., Mandi, M., Mathe, K., Töröcsik, B., Doczi, J., Turiak, L., Kiss, G., Konràd, C., Vajda, S., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-149898 · Cited by 103
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
The Mitochondrial Permeability Transition Pore Regulates Nitric Oxide-Mediated Apoptosis of Neurons Induced by Target Deprivation
Martin, L. J., Adams, N. A., Pan, Y., Price, A., & Wong, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2225-10.2011 · Cited by 96
The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94
Exercise triggers CAPN1-mediated AIF truncation, inducing myocyte cell death in arrhythmogenic cardiomyopathy
Chelko, S. P., Keceli, G., Carpi, A., Doti, N., Agrimi, J., Asimaki, A., Beti, C. B., Miyamoto, M., Amat-Codina, N., Bedja, D., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf0891 · Cited by 92
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
Self-citation
Molecular and biochemical changes of the cardiovascular system due to smoking exposure
Armani, C., Landini Jr., L., & Leone, A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787846973 · Cited by 68

Crucial Roles of Effectors in Interactions between Horticultural Crops and Pathogens
Liu, T., Chen, Y., Tian, S., et al. (2023) · Horticulturae · doi:10.3390/horticulturae9020250 · Cited by 9
20 Effector proteins of bacterial type III protein secretion systems: Elucidating their biochemical effects on eukaryotic signaling cascades
Orth, K., Dixon, J. E., & Bliska, J. B. (2002) · Methods in microbiology · doi:10.1016/s0580-9517(02)31021-3
Prediction of effector proteins and their implications in pathogenicity of phytopathogenic filamentous fungi: A review
Wu, Y., Xie, L., Jiang, Y., & Li, T. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.02.133 · Cited by 35
Remote homology clustering identifies lowly conserved families of effector proteins in plant-pathogenic fungi
Jones, D., Moolhuijzen, P., & Hane, J. K. (2021) · Microbial Genomics · doi:10.1099/mgen.0.000637 · Cited by 13
Microbial Pathogen Effectors in Plant Disease
Pelgrom, A. J. E., & den Ackerveken, G. F. J. M. V. (2016) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0023724 · Cited by 7

Authors: Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A.
Affiliations: University of Padua (IT)
Oregon Health & Science University (US)
ORCID: Bernardi, Paolo
Basso, Emy
Petronilli, Valeria
Forte, Michael A.
Venue: The FEBS Journal
Publisher: Wiley
Published: 2006-04-10
Volume: 273
Issue: 10
Pages: 2077-2099
ISSN: 1742-464X (ISSN-L)
1742-4658
DOI: 10.1111/j.1742-4658.2006.05213.x
OpenAlex: W2060605524
Cited by: 627
References: 276
Citations by year: 2026: 4 · 2025: 13 · 2024: 11 · 2023: 20 · 2022: 19 · 2021: 23 · 2020: 23 · 2019: 26 · 2018: 28 · 2017: 20 · 2016: 23 · 2015: 24 · 2014: 38 · 2013: 39 · 2012: 37
FWCI: 4.64
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Journal (publishedVersion)
PubMed (publishedVersion)
Padua Research Archive (University of Padova) (submittedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM069883, GM 69883)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
Keywords: mitochondrial permeability transition pore, inner mitochondrial membrane permeability, cell death, gene inactivation, pore structure, mitochondrial disease, in vivo disease models
MeSH terms: Mitochondrial Permeability Transition Pore, Animals, Humans, Liver Diseases, Muscular Diseases, Nervous System Diseases, Artifacts, Drug Delivery Systems, Myocardial Ischemia, Mitochondrial Membrane Transport Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The mitochondrial permeability transition from in vitro artifact to disease target

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks