The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
Abstract
Mitochondria play an important role in energy production, Ca2+ homeostasis and cell death. In recent years, the role of the mitochondria in apoptotic and necrotic cell death has attracted much attention. In apoptosis and necrosis, the mitochondrial permeability transition (mPT), which leads to disruption of the mitochondrial membranes and mitochondrial dysfunction, is considered to be one of the key events, although its exact role in cell death remains elusive. We therefore created mice lacking cyclophilin D (CypD), a protein considered to be involved in the mPT, to analyse its role in cell death. CypD-deficient mice were developmentally normal and showed no apparent anomalies, but CypD-deficient mitochondria did not undergo the cyclosporin A-sensitive mPT. CypD-deficient cells died normally in response to various apoptotic stimuli, but showed resistance to necrotic cell death induced by reactive oxygen species and Ca2+ overload. In addition, CypD-deficient mice showed a high level of resistance to ischaemia/reperfusion-induced cardiac injury. Our results indicate that the CypD-dependent mPT regulates some forms of necrotic death, but not apoptotic death.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“To date, peptidylprolyl isomerase F (PPIF; best known as cyclophilin D, CYPD) is the only protein whose in vivo requirement for MPT induction has been formally validated with robust genetic tools (although there is consensus around the notion that CYPD does not constitute the pore-forming unit of the PTPC) [376–379].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [377]
In the citing paper
“although there is consensus around the notion that CYPD does not constitute the pore-forming unit of the PTPC) [376–379].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [377]
In the citing paper
“Formation of the pore can occur in response to many stimuli, including Ca2+ overload and oxidant stress, but MPT does not play a role in all forms of apoptosis (46, 125, 309, 438).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [309]
In the citing paper
“Formation of the pore can occur in response to many stimuli, including Ca2+ overload and oxidant stress, but MPT does not play a role in all forms of apoptosis (46, 125, 309, 438).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [309]
In the citing paper
“In addition, in the absence of cyclophilin D, mice are more protected from cardiac damage after ischemia/reperfusion (25, 309);”
From Redox regulation of mitochondrial function (2012) · cites this paper as [309]
Citations
Cites
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,487
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Fischer, G., Wittmann‐Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F. X. (1989) · Nature · doi:10.1038/337476a0 · Cited by 1,408
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
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
Narita, M., Shimizu, S., Ito, T., Chittenden, T., Lutz, R. J., Matsuda, H., & Tsujimoto, Y. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14681 · Cited by 942
Self-citationFinucane, D., Bossy‐Wetzel, E., Waterhouse, N. J., Cotter, T. G., & Green, D. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2225 · Cited by 714
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–700 of 1,001
Mitochondrial factors with dual roles in death and survival
Cheng, W.-C., Berman, S., Ivanovska, I. L., Jonas, E. A., Lee, S., Chen, Y., Kaczmarek, L. K., Pineda, F. J., & Hardwick, J. M. (2006) · Oncogene · doi:10.1038/sj.onc.1209596 · Cited by 71
Tanwar, J., Singh, J. B., & Motiani, R. K. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.001 · Cited by 68
Kang, B. H., Tavecchio, M., Goel, H. L., Hsieh, C.-C., Garlick, D. S., Raskett, C. M., Lian, J. B., Stein, G. S., Languino, L. R., & Altieri, D. C. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.9 · Cited by 67
Calcium and Reactive Oxygen Species in Acute Pancreatitis: Friend or Foe?
Booth, D. M., Mukherjee, R., Sutton, R., & Criddle, D. N. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3983 · Cited by 69
Bcl-2 family-regulated apoptosis in health and disease
Kluck, R. M. (2010) · Cell Health and Cytoskeleton · doi:10.2147/chc.s6228 · Cited by 72
Shalbuyeva, N., Brustovetsky, T., & Brustovetsky, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702134200 · Cited by 70
Csukly, K., Ascah, A., Matas, J., Gardiner, P. F., Fontaine, E. M., & Burelle, Y. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109702 · Cited by 68
Cyclosporine in acute ischemic stroke
Nighoghossian, N., Berthezène, Y., Mechtouff, L., Derex, L., Cho, T., Ritzenthaler, T., Rheims, S., Chauveau, F., Béjot, Y., Jacquin, A., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000001639 · Cited by 68
Shore, E. R., Awais, M., Kershaw, N. M., Gibson, R. R., Pandalaneni, S. R., Latawiec, D., Li, W., Javed, M. A., Criddle, D. N., Berry, N. G., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01801 · Cited by 68
Cisplatin-induced necroptosis in TNFα dependent and independent pathways
Xu, Y., Ma, H., Fang, Y., Zhang, Z., Shao, J., Hong, M., Huang, C., Liu, J., & Chen, R. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.01.004 · Cited by 67
The molecular identity of the mitochondrial Ca2+ sequestration system
Starkov, A. A. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07756.x · Cited by 70
Lim, S. Y., Hausenloy, D. J., Arjun, S., Price, A. N., Davidson, S. M., Lythgoe, M. F., & Yellon, D. M. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01235.x · Cited by 67
Zhang, D., Lü, C., Whiteman, M., Chance, B., & Armstrong, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707528200 · Cited by 67
Phenotyping of an in Vitro Model of Ischemic Penumbra by iTRAQ-Based Shotgun Quantitative Proteomics
Datta, A., Park, J. E., Li, X., Zhang, H., Ho, Z. S., Heese, K., Lim, S. K., Tam, J. P., & Sze, S. K. (2009) · Journal of Proteome Research · doi:10.1021/pr900829h · Cited by 66
The consequences of mitochondrial amyloid β-peptide in Alzheimer's disease
Muirhead, K. E. A., Borger, E., Aitken, L., Conway, S. J., & Gunn‐Moore, F. J. (2010) · Biochemical Journal · doi:10.1042/bj20091941 · Cited by 68
Excitotoxins, Mitochondrial and Redox Disturbances in Multiple Sclerosis
Rajda, C., Pukoli, D., Bende, Z., Majláth, Z., & Vécsei, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020353 · Cited by 69
Lewis, A., Hayashi, T., Su, T.-P., & Betenbaugh, M. J. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9527-7 · Cited by 66
Necroptosis in heart disease: Molecular mechanisms and therapeutic implications
Guo, X., Chen, Y., & Liu, Q. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.05.006 · Cited by 70
Uo, T., Veenstra, T. D., & Morrison, R. S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6186-08.2009 · Cited by 67
Ischemia-Reperfusion-Induced Cardiac Injury
Powers, S. K., Murlasits, Z., Wu, M., & Kavazis, A. N. (2007) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3180d099c1 · Cited by 66
Small molecules, big effects: the role of microRNAs in regulation of cardiomyocyte death
Skommer, J., Rana, I., Marques, F. Z., Zhu, W., Du, Z., & Charchar, F. J. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.287 · Cited by 66
The Potential Role of Mitochondria in Pediatric Traumatic Brain Injury
Robertson, C., Soane, L., Siegel, Z. T. G., & Fiskum, G. M. (2006) · Developmental Neuroscience · doi:10.1159/000094169 · Cited by 67
The role of SIRT3 in mitochondrial homeostasis and cardiac adaptation to hypertrophy and aging
Sack, M. N. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.11.004 · Cited by 66
Antoniel, M., Giorgio, V., Fogolari, F., Glick, G. D., Bernardi, P., & Lippe, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15057513 · Cited by 68
Sánchez‐Duffhues, G., Calzado, M. A., de Vinuesa, A. G., Appendino, G., Fiebich, B. L., Loock, U., Lefarth‐Risse, A., Krohn, K., & Muñóz, E. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.01.004 · Cited by 65
Necroptosis: Who Knew There were so Many Interesting Ways to Die?
Fayaz, S. M., Kumar, V. S. S., & Rajanikant, G. K. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/18715273113126660189 · Cited by 65
Wu, J., Holstein, J. D., Upadhyay, G., Lin, D., Conway, S. J., Muller, E., & Lechleiter, J. D. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1256-07.2007 · Cited by 63
Regulation of mitochondrial ATP synthase in cardiac pathophysiology.
Long, Q., Yang, K., & Yang, Q. (2015) · Europe PMC (PubMed Central) · Cited by 64
What makes the mitochondria a killer? Can we condition them to be less destructive?
Murphy, E., & Steenbergen, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.003 · Cited by 67
Kajitani, K., Fujihashi, M., Kobayashi, Y., Shimizu, S., Tsujimoto, Y., & Miki, K. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21855 · Cited by 64
Self-citationSuperoxide flashes: Elemental events of mitochondrial ROS signaling in the heart
Wang, X., Jian, C., Zhang, X., Huang, Z., Xu, J., Hou, T., Shang, W. H., Ding, Y., Zhang, W., Ouyang, M., et al. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.02.007 · Cited by 65
Programmed necrosis in cardiomyocytes: mitochondria, death receptors and beyond
Zhang, J., Liu, D., Zhang, M., & Zhang, Y. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14363 · Cited by 67
The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release
Martinez‐Caballero, S., Dejean, L. M., Jonas, E. A., & Kinnally, K. W. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6570-z · Cited by 64
Programmed cell death in cardiac myocytes: strategies to maximize post-ischemic salvage
Mani, K. M. (2008) · Heart Failure Reviews · doi:10.1007/s10741-007-9073-7 · Cited by 64
Ceramide and mitochondria in ischemic brain injury.
Novgorodov, S. A., & Gudz, T. I. (2011) · Europe PMC (PubMed Central) · Cited by 62
Intertwined pathways of programmed cell death in immunity
Hedrick, S. Μ., Ch’en, I. L., & Alves, B. N. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00918.x · Cited by 66
Mishra, J., Davani, A. J., Natarajan, G. K., Kwok, W., Stowe, D. F., & Camara, A. K. S. (2019) · Cells · doi:10.3390/cells8091052 · Cited by 62
Mitochondria as therapeutic targets for cancer stem cells
Song, I. S. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i2.418 · Cited by 64
Sack, M. N. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00199.2011 · Cited by 64
Emter, C. A., & Baines, C. P. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00578.2010 · Cited by 64
Central role of mitochondrial injury in the pathogenesis of acute pancreatitis
Maléth, J., Rakonczay, Z., Venglovecz, V., Dolman, N. J., & Hegyi, P. J. (2012) · Acta Physiologica · doi:10.1111/apha.12037 · Cited by 63
Errakhi, R., Meimoun, P., Lehner, A., Vidal, G., Briand, J., Corbineau, F., Rona, J. P., & Bouteau, F. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/ern166 · Cited by 63
Synergistic effects of ion transporter and MAP kinase pathway inhibitors in melanoma
Eskiocak, U., Ramesh, V., Gill, J. G., Zhao, Z., Yuan, S. W., Wang, M., Vandergriff, T. W., Shackleton, M. J., Quintana, E., Frankel, A. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms12336 · Cited by 62
Luo, Y., Benjanuwattra, J., Chattipakorn, S. C., & Chattipakorn, N. (2020) · Acta Physiologica · doi:10.1111/apha.13541 · Cited by 65
“Simple but not simpler”: toward a unified picture of energy requirements in cell death
Chiarugi, A. (2005) · The FASEB Journal · doi:10.1096/fj.05-4200rev · Cited by 62
Mitochondrial Biogenesis and Function in Arabidopsis†
Millar, A. H., Small, I., Day, D. A., & Whelan, J. (2008) · The Arabidopsis Book · doi:10.1199/tab.0111 · Cited by 68
Mitochondrial Transfer as a Therapeutic Strategy Against Ischemic Stroke
Chen, W., Huang, J., Hu, Y., Khoshnam, S. E., & Sarkaki, A. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00828-7 · Cited by 62
The role of hexokinase in cardioprotection – mechanism and potential for translation
Halestrap, A. P., Pereira, G. C., & Pasdois, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12899 · Cited by 62
Morin, D., Assaly, R., Paradis, S., & Berdeaux, A. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709789712871 · Cited by 64
Dysregulated mitochondrial Ca2+ and ROS signaling in skeletal muscle of ALS mouse model
Zhou, J., Li, A., Li, X., & Yi, J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.024 · Cited by 59
What is the nature of the mitochondrial permeability transition pore and What is it Not?
Siemen, D., & Ziemer, M. (2013) · IUBMB Life · doi:10.1002/iub.1130 · Cited by 62
Integration of calcium with the signaling network in cardiac myocytes
SCHAUB, M. C., Hefti, M. A., & Zaugg, M. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.04.005 · Cited by 61
Rip3 knockdown rescues photoreceptor cell death in blind pde6c zebrafish
viringipurampeer, I. A., Shan, X., Gregory-Evans, K., Zhang, J. P., Mohammadi, Z., & Gregory, C. Y. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2013.191 · Cited by 61
Chelerythrine Induces Apoptosis through a Bax/Bak-independent Mitochondrial Mechanism
Wan, K. F., Chan, S. L., Sukumaran, S. K., Lee, M., & Yu, V. C. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707687200 · Cited by 61
Pagel, P. S. (2008) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2008.03.005 · Cited by 62
Zhang, B., Liu, S.-Q., Li, C., Lykken, E. A., Jiang, S., Wong, E., Gong, Z., Tao, Z., Zhu, B., Wan, Y., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.007 · Cited by 62
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 63
Bøtker, H. E., Cabrera-Fuentes, H. A., Ruiz‐Meana, M., Heusch, G., & Ovize, M. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14953 · Cited by 61
Mitochondria and heart failure: new insights into an energetic problem.
Chen, L., & Knowlton, A. A. (2010) · PubMed · Cited by 62
BH3-only proteins trigger cytochrome c release, but how?
Häcker, G. A., & Weber, A. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.12.022 · Cited by 61
From bioblasts to mitochondria: ever expanding roles of mitochondria in cell physiology
O'Rourke, B. P. (2010) · Frontiers in Physiology · doi:10.3389/fphys.2010.00007 · Cited by 66
Mechanisms of postischemic cardiac death and protection following myocardial injury
Mastoor, Y., Murphy, E., & Román, B. (2025) · Journal of Clinical Investigation · doi:10.1172/jci184134 · Cited by 68
Clustering of Stimuli on Single-Walled Carbon Nanotube Bundles Enhances Cellular Activation
Fadel, T. R., Look, M., Staffier, P. A., Haller, G. L., Pfefferle, L. D., & Fahmy, T. M. (2009) · Langmuir · doi:10.1021/la902068z · Cited by 60
McGee, A. M., & Baines, C. P. (2010) · Biochemical Journal · doi:10.1042/bj20101431 · Cited by 63
Watanabe, T., Otsu, K., Takeda, T., Yamaguchi, O., Hikoso, S., Kashiwase, K., Higuchi, Y., Taniike, M., Nakai, A., Matsumura, Y., et al. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.151 · Cited by 60
Self-citationPRC2 loss induces chemoresistance by repressing apoptosis in T cell acute lymphoblastic leukemia
Ariës, I. M., Bodaar, K., Karim, S., Chonghaile, T. N., Hinze, L., Burns, M., Pfirrmann, M., Degar, J., Landrigan, J., Balbach, S. T., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20180570 · Cited by 60
Carraro, M., Jones, K., Sartori, G., Schiavone, M., Antonucci, S., Kucharczyk, R., di Rago, J., Franchin, C., Arrigoni, G., Forte, M. A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108095 · Cited by 61
On the structural possibility of pore-forming mitochondrial F o F 1 ATP synthase
Gerle, C. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.008 · Cited by 57
Angeli, S., Foulger, A., Chamoli, M., Peiris, T. H., Gerencser, A. A., Shahmirzadi, A. A., Andersen, J. K., & Lithgow, G. J. (2021) · eLife · doi:10.7554/elife.63453 · Cited by 57
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 72
Matas, J., Young, N. T. S., Bourcier‐Lucas, C., Ascah, A., Marcil, M., Deschepper, C. F., & Burelle, Y. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.10.020 · Cited by 59
Argaud, L., Gateau-Roesch, O., Augeul, L., Couture-Lepetit, E., Loufouat, J., Gomez, L., Robert, D., & Ovize, M. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01035.2007 · Cited by 61
Luvisetto, S., Basso, E., Petronilli, V., Bernardi, P., & Forte, M. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.030 · Cited by 61
Arokium, H., Ouerfelli, H., Velours, G., Camougrand, N. M., Vallette, F. M., & Manon, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704891200 · Cited by 59
Cellular and molecular pathways to myocardial necrosis and replacement fibrosis
Gandhi, M. S., Kamalov, G., Shahbaz, A. U., Bhattacharya, S. K., Ahokas, R. A., Sun, Y., Gerling, I., & Weber, K. T. (2010) · Heart Failure Reviews · doi:10.1007/s10741-010-9169-3 · Cited by 59
Programmed death as a therapeutic target to reduce myocardial infarction
Webster, K. A. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.07.004 · Cited by 59
Targeting Mitochondria in Fighting Cancer
Gogvadze, V. G. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798764933 · Cited by 59
Zhang, J., Ma, G., Guo, Z., Yu, Q., Han, L., Han, M., & Zhu, Y. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.06.032 · Cited by 59
Gukovskaya, A. S., & Gukovsky, I. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.04.025 · Cited by 60
Menazza, S., Wong, R. P., Nguyen, T. T. M., Wang, G., Guček, M., & Murphy, E. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.12.004 · Cited by 58
MAC and Bcl-2 family proteins conspire in a deadly plot
Dejean, L. M., Ryu, S. Y., Martinez‐Caballero, S., Teijido, Ó., Peixoto, P. M. V., & Kinnally, K. W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.007 · Cited by 57
Sharma, A. K., Singh, V., Gera, R., Purohit, M. P., & Ghosh, D. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0133-7 · Cited by 58
Targeting immunometabolism in host defence against Mycobacterium tuberculosis
Sheedy, F. J., & Divangahi, M. (2020) · Immunology · doi:10.1111/imm.13276 · Cited by 62
Gong, Y., Lin, J., Ma, Z., Yu, M., Wang, M., Lai, D., & Fu, G. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119511 · Cited by 58
Mitochondrial permeability transition pore: Back to the drawing board
Chinopoulos, C. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.010 · Cited by 57
Luo, Y., Li, Z., Ge, P., Guo, H., Li, L., Zhang, G., Xu, C., & Chen, H. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s310990 · Cited by 57
Li, P., Dong, X., Zhang, B., Zhang, X., Liu, J.-Z., Ma, D., & Ma, L. (2021) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001772 · Cited by 56
Bax Regulates Neuronal Ca2+Homeostasis
D’Orsi, B., Kilbride, S. M., Chen, G., Perez‐Alvarez, S., Bonner, H. P., Pfeiffer, S., Plesnila, N., Engel, T., Henshall, D. C., Düßmann, H., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2453-14.2015 · Cited by 59
Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones
Kang, B. H., & Altieri, D. C. (2009) · Oncogene · doi:10.1038/onc.2009.227 · Cited by 57
Thomas, B., Banerjee, R., Starkova, N. N., Zhang, S. F., Calingasan, N. Y., Yang, L., Wille, E. J., Lorenzo, B. J., Ho, D. J., Beal, M. F., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3849 · Cited by 58
Dumas, J., Argaud, L., Cottet‐Rousselle, C., Vial, G., Dahout-Gonzalez, C., Détaille, D., Leverve, X. M., & Fontaine, E. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900926200 · Cited by 61
Park, J. S., Pasupulati, R., Feldkamp, T., Roeser, N. F., & Weinberg, J. M. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00033.2011 · Cited by 57
Papanicolaou, K. N., Phillippo, M. M., & Walsh, K. X. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00185.2012 · Cited by 57
F‐ ATP synthase and the permeability transition pore: fewer doubts, more certainties
Carraro, M., Checchetto, V., Szabó, I., & Bernardi, P. (2019) · FEBS Letters · doi:10.1002/1873-3468.13485 · Cited by 59
Developmental Effects of Sublethal Mitochondrial Injury in Mouse Oocytes1
Thouas, G. A., Trounson, A. O., & Jones, G. M. (2006) · Biology of Reproduction · doi:10.1095/biolreprod.105.048611 · Cited by 57
Tojo, K., Tamada, N., Nagamine, Y., Yazawa, T., Ota, S., & Goto, T. (2017) · The FASEB Journal · doi:10.1096/fj.201700888r · Cited by 57
Targeting the Calcium Signalling Machinery in Cancer
Bruce, J. I. E., & James, A. D. (2020) · Cancers · doi:10.3390/cancers12092351 · Cited by 59
Forini, F., Nicolini, G., & Iervasi, G. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16036312 · Cited by 57
Mitochondrial calcium handling during ischemia-induced cell death in neurons
Gouriou, Y., Demaurex, N., Bijlenga, P., & Marchi, U. D. (2011) · Biochimie · doi:10.1016/j.biochi.2011.08.001 · Cited by 55
Nishikawa, S., Tatsumi, T., Shiraishi, J., Matsunaga, S., Takeda, M., Mano, A., Kobara, M., Keira, N., Okigaki, M., & Takahashi, T. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.01.020 · Cited by 56
Metadata
- Authors
- Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y.
- Affiliations
- Laboratory of Molecular Genetics (PL)
- Japan Science and Technology Agency (JP)
- The University of Osaka (JP)
- Corresponding author
- Tsujimoto, Yoshihide
- ORCID
- Venue
- Nature
- Published
- 2005-03
- Volume
- 434
- Issue
- 7033
- Pages
- 652-658
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2063099262
- Cited by
- 1,635
- References
- 32
- Citations by year
- 2026: 27 · 2025: 40 · 2024: 32 · 2023: 42 · 2022: 47 · 2021: 54 · 2020: 55 · 2019: 58 · 2018: 73 · 2017: 70 · 2016: 77 · 2015: 74 · 2014: 119 · 2013: 81 · 2012: 115
- FWCI
- 41.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- cyclophilin D, mitochondrial permeability transition, necrosis, apoptosis, cyclosporine, reactive oxygen species, calcium overload, ischemia-reperfusion injury, cardiac injury, mitochondrial dysfunction
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Animals, Calcium, Cells, Cultured, Enzyme Activation, Fibroblasts, Hydrogen Peroxide, Mitochondria, Liver, Mitochondrial Swelling, Necrosis, Thymus Gland, Myocardial Reperfusion Injury, Myocardial Ischemia, Apoptosis, Reactive Oxygen Species, Mice, Knockout, Caspases, Cyclophilins, Hepatocytes, Mice
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