Mitochondrial membrane permeability transition and cell death
Open accessAbstract
Mitochondria are important organelles for energy production, Ca2+ homeostasis, and cell death. In recent years, the role of the mitochondria in both apoptotic and necrotic cell death has received much attention. In apoptotic and necrotic death, an increase of mitochondrial membrane permeability is considered to be one of the key events, although the detailed mechanism remains to be elucidated. The mitochondrial membrane permeability transition (MPT) is a Ca2+-dependent increase in the permeability of the mitochondrial membrane that leads to loss of Deltapsi, mitochondrial swelling, and rupture of the outer mitochondrial membrane. The MPT is thought to occur after the opening of a channel, which is termed the permeability transition pore (PTP) and putatively consists of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocator (ANT), cyclophilin D (Cyp D: a mitochondrial peptidyl prolyl-cis, trans-isomerase), and other molecule(s). Our studies of mice lacking Cyp D have revealed that it is essential for occurrence of the MPT and that the Cyp D-dependent MPT regulates some forms of necrotic cell death, but not apoptotic death. We have also shown that two anti-apoptotic proteins, Bcl-2 and Bcl-x(L), block the MPT by directly inhibition of VDAC activity. Here we summarize a role of the MPT in cell death.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The MPT pore is formed by structural molecules including VDAC, ANT, and CyPD.
“The MPT pore is a protein pore formed by structural molecules such as voltage-dependent anion channel, ANT, and cyclophilin D (CyPD) (Tsujimoto et al., 2006).”
From Mitochondrial Dysfunction Induced by Sertraline, an Antidepressant Agent (2012) · cites this paper as Tsujimoto et al., 2006
Section 2 (page not provided) says the MPT pore is thought to be a channel complex consisting of VDAC, ANT, Cyp D and other molecules, but explicitly says its exact nature remains undetermined. Section 3 further reports that MPT occurs in mice lacking ANT1 and ANT2. The citing sentence names the proposed components correctly but presents their structural role as established rather than putative. (LLM, conf=0.90)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,416 · see citing works
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,395 · see citing works
(2001) · PubMed · Cited by 2,381 · see citing works
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works
Mitochondria as the central control point of apoptosis
Desagher, S., & Martinou, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,915 · see citing works
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635 · see citing works
Self-citationMitochondrial control of nuclear apoptosis.
Zamzami, N., Susín, S. A., Marchetti, P., Hirsch, T., Gomez-Monterrey, I. M., Castedo, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1533 · Cited by 1,360 · see citing works
Newmeyer, D. D., & Ferguson-Miller, S. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00116-8 · Cited by 1,268 · see citing works
Green, D. R., & Evan, G. I. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00024-7 · Cited by 1,254 · see citing works
Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis
Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168 · see citing works
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · see citing works
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 · see citing works
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 1,029 · see citing works
The biochemistry of programmed cell death
Kroemer, G., PETIT, P. X., Zamzami, N., Vayssière, J., & Mignotte, B. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.13.7557017 · Cited by 992 · see citing works
Life-or-death decisions by the Bcl-2 protein family
Adams, J. M., & Cory, S. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01740-0 · Cited by 887 · see citing works
Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., Hetz, C., Danial, N. N., Moskowitz, M. A., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505294102 · Cited by 820 · see citing works
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · see citing works
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 · see citing works
Broekemeier, K. M., Dempsey, M. E., & Pfeiffer, D. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83116-7 · Cited by 699 · see citing works
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 · see citing works
Cell death regulation by the Bcl‐2 protein family in the mitochondria
Tsujimoto, Y. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10254 · Cited by 497 · see citing works
Self-citationCrompton, M., Virji, S., & Ward, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580729.x · Cited by 492 · see citing works
He, L., & Lemasters, J. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03314-2 · Cited by 435 · see citing works
Bcl-2 prevents apoptotic mitochondrial dysfunction by regulating proton flux
Shimizu, S., Eguchi, Y., Kamiike, W., Funahashi, Y., Mignon, A., Lacronique, V., Matsuda, H., & Tsujimoto, Y. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1455 · Cited by 410 · see citing works
Self-citationWoodfield, K., Rück, A., Brdiczka, D. G., & Halestrap, A. P. (1998) · Biochemical Journal · doi:10.1042/bj3360287 · Cited by 386 · see citing works
Essential Role of Voltage-Dependent Anion Channel in Various Forms of Apoptosis in Mammalian Cells
Shimizu, S., Matsuoka, Y., Shinohara, Y., Yoneda, Y., & Tsujimoto, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.2.237 · Cited by 367 · see citing works
Self-citationPeptidylproline cis/trans isomerases
Gałat, A., & Metcalfe, S. M. (1995) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(94)00009-x · Cited by 240 · see citing works
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 · see citing works
Cyclophilin D, a Component of the Permeability Transition-Pore, Is an Apoptosis Repressor
Schubert, A., & Grimm, S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-0476 · Cited by 128 · see citing works
On the Involvement of Mitochondrial Intermembrane Junctional Complexes in Apoptosis
Crompton, M. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457197 · Cited by 77 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693 · see citing works
Mitochondria, oxidative metabolism and cell death in stroke
Sims, N. R., & Muyderman, H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.003 · Cited by 675 · see citing works
Mitochondrial fusion, fission and autophagy as a quality control axis: The bioenergetic view
Twig, G., Hyde, B. B., & Shirihai, O. S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.05.001 · Cited by 646 · see citing works
Oxidative stress and left ventricular remodelling after myocardial infarction
Hori, M., & Nishida, K. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn335 · Cited by 525 · see citing works
When ER stress reaches a dead end
Urra, H., Dufey, E., Lisbona, F., Rojas‐Rivera, D., & Hetz, C. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.024 · Cited by 458 · see citing works
Mitochondrial morphology transitions and functions: implications for retrograde signaling?
Picard, M. A., Shirihai, O. S., Gentil, B. J., & Burelle, Y. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00584.2012 · Cited by 320 · see citing works
Mitochondrial Channels: Ion Fluxes and More
Szabó, I., & Zoratti, M. (2014) · Physiological Reviews · doi:10.1152/physrev.00021.2013 · Cited by 321 · see citing works
Webster, K. A. (2012) · Future Cardiology · doi:10.2217/fca.12.58 · Cited by 301 · see citing works
Bai, J., & Lyden, P. D. (2015) · International Journal of Stroke · doi:10.1111/ijs.12434 · Cited by 272 · see citing works
Mitochondria in Neurodegeneration
Lezi, E., & Swerdlow, R. H. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_12 · Cited by 204 · see citing works
Recent Progress in Mitochondria-Targeted Drug and Drug-Free Agents for Cancer Therapy
Jeena, M. T., Kim, S., Jin, S., & Ryu, J. (2019) · Cancers · doi:10.3390/cancers12010004 · Cited by 166 · see citing works
Champattanachai, V., Marchase, R. B., & Chatham, J. C. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00456.2007 · Cited by 153 · see citing works
Baumann, S., Fas, S. C., Giaisi, M., Müller, W. W., Merling, A., Gülow, K., Edler, L., Krammer, P. H., & Li‐Weber, M. (2007) · Blood · doi:10.1182/blood-2007-06-096198 · Cited by 150 · see citing works
Central roles of apoptotic proteins in mitochondrial function
Kilbride, S. M., & Prehn, J. H. M. (2012) · Oncogene · doi:10.1038/onc.2012.348 · Cited by 147 · see citing works
Mitochondrial morphology transition is an early indicator of subsequent cell death in Arabidopsis
Scott, I., & Logan, D. C. (2007) · New Phytologist · doi:10.1111/j.1469-8137.2007.02255.x · Cited by 144 · see citing works
Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis
Groves, J. A., Lee, A., Yildirir, G., & Zachara, N. E. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0426-y · Cited by 143 · see citing works
Yuan, H., Gerencser, A. A., Liot, G., Lipton, S. A., Ellisman, M. H., Perkins, G. A., & Bossy‐Wetzel, E. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402046 · Cited by 140 · see citing works
Sun, J., Li, Y., Ding, Y., Wang, J., Geng, J., Yang, H., Ren, J., Tang, J., & Gao, J. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.039 · Cited by 138 · see citing works
In vitro and in vivo anticancer activity of steroid saponins of Paris polyphylla var. yunnanensis.
Yan, L., Zhang, Y. J., Gao, W., Man, S., & Wang, Y. (2009) · PubMed · Cited by 135 · see citing works
Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia
Viganò, A., Ripamonti, M., Palma, S. D., Capitanio, D., Vasso, M., Wait, R., Lundby, C., Cerretelli, P., & Gelfi, C. (2008) · PROTEOMICS · doi:10.1002/pmic.200800232 · Cited by 126 · see citing works
Mitochondrial Thiols in the Regulation of Cell Death Pathways
Yin, F., Sancheti, H., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4639 · Cited by 112 · see citing works
Biogenesis of mitochondrial outer membrane proteins
Walther, D. M., & Rapaport, D. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.04.013 · Cited by 121 · see citing works
Mitochondrial Dysfunction Induced by Sertraline, an Antidepressant Agent
Li, Y., Couch, L., Higuchi, M., Fang, J.-L., & Guo, L. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs100 · Cited by 120 · see citing works
The Neurodegenerative Mitochondriopathies
Swerdlow, R. H. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1095 · Cited by 112 · see citing works
Investigating Drug-induced Mitochondrial Toxicity: A Biosensor to Increase Drug Safety?
Pereira, C., Moreira, A. C., Pereira, S. P., Machado, N. J., Carvalho, F. S., Sardão, V. A., & Oliveira, P. J. (2009) · Current Drug Safety · doi:10.2174/157488609787354440 · Cited by 105 · see citing works
Hakiminia, B., Alikiaii, B., Khorvash, F., & Mousavi, S. (2022) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12767 · Cited by 104 · see citing works
Jensen, R. V., Zachara, N. E., Nielsen, P. H., Kimose, H., Kristiansen, S. B., & Bøtker, H. E. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs337 · Cited by 100 · see citing works
Probing the Outer Mitochondrial Membrane in Cardiac Mitochondria with Nanoparticles
Salnikov, V. V., Lukyanenko, Y., Frederick, C. A., Lederer, W. J., & Lukyanenko, V. I. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.094318 · Cited by 100 · see citing works
Voltage-dependent anion channels are a key factor of male fertility
Kwon, W., Park, Y.-J., Mohamed, E. A., & Pang, M. (2012) · Fertility and Sterility · doi:10.1016/j.fertnstert.2012.09.021 · Cited by 99 · see citing works
Mitochondrial control of cell death induced by hyperosmotic stress
Criollo, A., Galluzzi, L., Maiuri, M. C., Tasdemir, E., Lavandero, S., & Kroemer, G. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0328-x · Cited by 96 · see citing works
Lin, P., Lin, H., Kuo, C.-C., & Yang, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0152-0 · Cited by 95 · see citing works
Reperfusion Promotes Mitochondrial Dysfunction following Focal Cerebral Ischemia in Rats
Li, J., Ma, X., Yu, W., Lou, Z., Mu, D., Wang, Y., Shen, B., & Qi, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046498 · Cited by 92 · see citing works
Ott, L. W., Resing, K. A., Sizemore, A. W., Heyen, J. W., Cocklin, R., Pedrick, N. M., Woods, H. C., Chen, J. Y., Goebl, M. G., Witzmann, F. A., et al. (2007) · Journal of Proteome Research · doi:10.1021/pr060665l · Cited by 87 · see citing works
Majors, B. S., Betenbaugh, M. J., & Chiang, G. G. (2007) · Metabolic Engineering · doi:10.1016/j.ymben.2007.05.003 · Cited by 87 · see citing works
Multiple roles of microsomal glutathione transferase 1 in cellular protection: A mechanistic study
Johansson, K., Järvliden, J., Gogvadze, V. G., & Morgenstern, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.013 · Cited by 85 · see citing works
Wang, Y., Li, Y., Xue, H., Pritchard, H. W., & Wang, X. (2014) · The Plant Journal · doi:10.1111/tpj.12737 · Cited by 85 · see citing works
Tarantino, G., Finelli, C., Scopacasa, F., Pasanisi, F., Contaldo, F., Capone, D., & Savastano, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/920676 · Cited by 80 · see citing works
Mondal, N. K., Behera, J., Kelly, K. E., George, A. K., Tyagi, P., & Tyagi, N. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.11.015 · Cited by 78 · see citing works
Sung, K., Odinokova, I. V., Mareninova, O. A., Rakonczay, Z., Hegyi, P. J., Pandol, S. J., Gukovsky, I., & Gukovskaya, A. S. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.01.009 · Cited by 78 · see citing works
Immunoregulatory role of melatonin in cancer
Moradkhani, F., Moloudizargari, M., Fallah, M., Asghari, N., Khoei, H. H., & Asghari, M. H. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29036 · Cited by 79 · see citing works
Kang, B. H. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.1.1 · Cited by 74 · see citing works
Nie, S., Yue, H., Zhou, J. M., & Xing, D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119853 · Cited by 73 · see citing works
Siu, P. M. (2009) · Frontiers in bioscience · doi:10.2741/3253 · Cited by 71 · see citing works
Nmnat3 Is Dispensable in Mitochondrial NAD Level Maintenance In Vivo
Yamamoto, M., Hikosaka, K., Mahmood, A., Tobe, K., Shojaku, H., Inohara, H., & Nakagawa, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147037 · Cited by 70 · see citing works
Self-citationHua, X., & Wang, D. (2022) · Reviews of Environmental Contamination and Toxicology · doi:10.1007/s44169-022-00013-x · Cited by 71 · see citing works
Acrolein induces selective protein carbonylation in synaptosomes
Mello, C. F., Rukhsana Sultana, A., Piroddi, M., Cai, J., Pierce, W. M. J., Klein, J. B., & Butterfield, D. A. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.04.003 · Cited by 67 · see citing works
Cellular targets of natural products
Dixon, N., Wong, L. S., Geerlings, T. H., & Micklefield, J. (2007) · Natural Product Reports · doi:10.1039/b616808f · Cited by 64 · see citing works
Morin, D., Assaly, R., Paradis, S., & Berdeaux, A. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709789712871 · Cited by 62 · see citing works
Melatonin enhances hydrogen peroxide-induced apoptosis in human promyelocytic leukaemia HL-60 cells
Bejarano, I., Espino, J., Marchena, A. M., Barriga, C., Paredes, S. D., Rodríguez, A. B., & Pariente, J. A. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0783-8 · Cited by 62 · see citing works
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 59 · see citing works
Kim, C., & Choi, K. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119607 · Cited by 64 · see citing works
Revisiting Regulated Cell Death Responses in Viral Infections
Balaya, R. D. A., Prasad, T. S. K., & Kandasamy, R. K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137023 · Cited by 59 · see citing works
Luvisetto, S., Basso, E., Petronilli, V., Bernardi, P., & Forte, M. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.030 · Cited by 59 · see citing works
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 · see citing works
p66SHC-mediated mitochondrial dysfunction in renal proximal tubule cells during oxidative injury
Arany, I., Faisal, A., Clark, J. S., Vera, T., Baliga, R., & Nagamine, Y. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00639.2009 · Cited by 57 · see citing works
Cui, Y., Zhang, H., Ji, M., Jia, M., Chen, H., Yang, J., & Duan, M. (2014) · Journal of Surgical Research · doi:10.1016/j.jss.2014.05.060 · Cited by 58 · see citing works
Panov, A. V., & Orynbayeva, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072078 · Cited by 58 · see citing works
Identification of new tyrosine phosphorylated proteins in rat brain mitochondria
Lewandrowski, U., Sickmann, A., Cesaro, L., Brunati, A. M., Toninello, A., & Salvi, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.077 · Cited by 58 · see citing works
MEK inhibition suppresses the development of lung fibrosis in the bleomycin model
Galuppo, M., Esposito, E., Mazzon, E., Paola, R. D., Paterniti, I., Impellizzeri, D., & Cuzzocrea, S. (2011) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-011-0637-7 · Cited by 53 · see citing works
Li, J., Yu, W., Li, X., Qi, S.-H., & Li, B. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.029 · Cited by 53 · see citing works
Shibuya, T., & Tsujimoto, Y. (2012) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2012.08.005 · Cited by 52 · see citing works
Self-citationMeclizine-induced enhanced glycolysis is neuroprotective in Parkinson disease cell models
Hong, C., Chau, K., & Schapira, A. H. V. (2016) · Scientific Reports · doi:10.1038/srep25344 · Cited by 52 · see citing works
Reis, Y., Bernardo-Faura, M., Richter, D., Wolf, T. A., Brors, B., Hamacher‐Brady, A., Eils, R., & Brady, N. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028694 · Cited by 51 · see citing works
Targeting Apoptosis in Autoimmune Hepatitis
Czaja, A. J. (2014) · Digestive Diseases and Sciences · doi:10.1007/s10620-014-3284-2 · Cited by 50 · see citing works
Queiroga, C. S. F., Tomasi, S., Widerøe, M., Alves, P. M., Vercelli, A., & Vieira, H. L. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042632 · Cited by 49 · see citing works
The Apoptosome: Emerging Insights and New Potential Targets for Drug Design
D’Amelio, M., Tino, E., & Cecconi, F. (2007) · Pharmaceutical Research · doi:10.1007/s11095-007-9396-z · Cited by 48 · see citing works
Harada, T., Sada, R., Osugi, Y., Matsumoto, S., Matsuda, T., Hayashi, M., Nagai, T., Harada, A., & Kikuchi, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.249045 · Cited by 49 · see citing works
Kicińska, A., Świda-Barteczka, A., Bednarczyk, P., Koszela-Piotrowska, I., Choma, K., Dołowy, K., Szewczyk, A. M., & Jarmuszkiewicz, W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701496200 · Cited by 48 · see citing works
Redox modulation and human bile duct cancer inhibition by curcumin
Suphim, B., Prawan, A., Kukongviriyapan, U., Kongpetch, S., Buranrat, B., & Kukongviriyapan, V. (2010) · Food and Chemical Toxicology · doi:10.1016/j.fct.2010.05.059 · Cited by 46 · see citing works
Han, J., Goldstein, L. A., Hou, W., Froelich, C. J., Watkins, S. C., & Rabinowich, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086587 · Cited by 46 · see citing works
Identification of thioredoxin-2 as a regulator of the mitochondrial permeability transition.
He, M., Cai, J.-Y., Go, Y., Johnson, J. M., Martin, W. D., Hansen, J. M., & Jones, D. P. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn116 · Cited by 48 · see citing works
Sarkey, J. P., Chu, M.-S., McShane, M., Bovo, E., Mou, Y. A., Zima, A., de Tombe, P., Kartje, G. L., & Martin, J. L. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.03.004 · Cited by 45 · see citing works
Carnosic Acid as a Promising Agent in Protecting Mitochondria of Brain Cells
de Oliveira, M. R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0842-6 · Cited by 45 · see citing works
Nishida, K., & Otsu, K. (2008) · Circulation Journal · doi:10.1253/circj.cj-08-0669 · Cited by 44 · see citing works
Szigeti, A., Hocsák, E., Rapolti, E., Rácz, B., Boronkai, Á., Pozsgai, É., Debreceni, B., Bognár, Z., Bellyei, S., Sümegi, B., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015222 · Cited by 43 · see citing works
Therapeutic targets in the mitochondrial apoptotic pathway
Häcker, G. A., & Paschen, S. A. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.4.515 · Cited by 42 · see citing works
Singh, P. K., Deorukhkar, A., Venkatesulu, B. P., Li, X., Tailor, R. C., Bomalaski, J. S., & Krishnan, S. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0708 · Cited by 39 · see citing works
Lynn, B. C., Wang, J., Markesbery, W. R., & Lovell, M. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1254 · Cited by 37 · see citing works
Gubellini, P., Picconi, B., Filippo, M. D., & Calabresi, P. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.001 · Cited by 37 · see citing works
Interaction of mitochondrial potassium channels with the permeability transition pore
Cheng, Y. D., Dębska–Vielhaber, G., & Siemen, D. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.038 · Cited by 36 · see citing works
Feldkamp, T., Park, J. S., Pasupulati, R., Amora, D. N., Roeser, N. F., Venkatachalam, M. A., & Weinberg, J. M. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00422.2009 · Cited by 35 · see citing works
Fang, N., Yao, Y.-T., Shi, C., & Li, L. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0030-5 · Cited by 35 · see citing works
Role of MGST1 in reactive intermediate-induced injury
Schaffert, C. S. (2011) · World Journal of Gastroenterology · doi:10.3748/wjg.v17.i20.2552 · Cited by 34 · see citing works
Velásquez, E., Nogueira, F. C. S., Velásquez, I., Schmitt, A., Falkai, P., Domont, G. B., & Martins‐de‐Souza, D. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00422 · Cited by 33 · see citing works
Naranmandura, H., Chen, X., Tanaka, M. H., Wang, W., Rehman, K., Xu, S., Chen, Z., Chen, S. Q., & Suzuki, N. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs154 · Cited by 33 · see citing works
Omi / HtrA2 is relevant to the selective vulnerability of striatal neurons in Huntington’s disease
Inagaki, R., Tagawa, K., Qi, M., Enokido, Y., Ito, H., Tamura, T., Shimizu, S., Oyanagi, K., Arai, N., Kanazawa, I., et al. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06323.x · Cited by 33 · see citing works
Self-citationBcl-2 Protects Tubular Epithelial Cells from Ischemia Reperfusion Injury by Inhibiting Apoptosis
Suzuki, C., Isaka, Y., Shimizu, S., Tsujimoto, Y., Takabatake, Y., Ito, T., Takahara, S., & Imai, E. (2008) · Cell Transplantation · doi:10.3727/000000008783907053 · Cited by 32 · see citing works
Self-citationGao, W., Li, D., Cai, D.-E., Huang, X., Zheng, B., Huang, Y., Chen, Z.-X., & Wang, X. (2016) · Oncology Reports · doi:10.3892/or.2016.5225 · Cited by 31 · see citing works
Dynamic Behavior of Double-Membrane-Bounded Organelles in Plant Cells
Takagi, S., Islam, M. S., & Iwabuchi, K. (2011) · International review of cytology · doi:10.1016/b978-0-12-385859-7.00004-5 · Cited by 31 · see citing works
Renton, J. P., Xu, N., Clark, J. J., & Hansen, M. R. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22381 · Cited by 31 · see citing works
Baliga, S. S., Schunke, K. J., Hadzimichalis, N. M., Golfetti, R., & Merrill, G. F. (2010) · Brain Research · doi:10.1016/j.brainres.2010.01.013 · Cited by 28 · see citing works
Sun, S., Pan, S., Miao, A., Ling, C., Shi, P., Tang, J., Chen, D., & Zhao, C. (2013) · Oncology Reports · doi:10.3892/or.2013.2504 · Cited by 27 · see citing works
Dehydroeburicoic Acid Induces Calcium- and Calpain-Dependent Necrosis in Human U87MG Glioblastomas
Deng, J.-Y., Chen, S.-J., Jow, G., Hsueh, C.-W., & Jeng, C. (2009) · Chemical Research in Toxicology · doi:10.1021/tx9002275 · Cited by 27 · see citing works
Cell Death in Brain Development and Degeneration: Control of Caspase Expression May Be Key!
Madden, S. D., & Cotter, T. G. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8021-4 · Cited by 27 · see citing works
Murasawa, S., Iuchi, K., Sato, S., Noguchi‐Yachide, T., Sodeoka, M., Yokomatsu, T., Dodo, K., Hashimoto, Y., & Aoyama, H. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.08.062 · Cited by 26 · see citing works
Mozaffari, M. S., & Schaffer, S. W. (2008) · American Journal of Hypertension · doi:10.1038/ajh.2008.25 · Cited by 26 · see citing works
Ravera, S., Bonifacino, T., Bartolucci, M., Milanese, M., Gallia, E., Provenzano, F., Cortese, K., Panfoli, I., & Bonanno, G. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1059-z · Cited by 25 · see citing works
Chang, S. S., Jiang, W. W., Smith, I., Glazer, C. A., Sun, W., Mithani, S. K., & Califano, J. A. (2009) · International Journal of Cancer · doi:10.1002/ijc.24777 · Cited by 25 · see citing works
Li, X., Wen, W., Li, P., Fu, Y., Chen, H., Wang, F., Dai, Y., & Xu, S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5590745 · Cited by 24 · see citing works
Liu, C., Huang, Y., Zhang, Y., Chen, X., Kong, X., & Dong, Y. (2017) · Free Radical Research · doi:10.1080/10715762.2017.1289376 · Cited by 24 · see citing works
- Authors
- Tsujimoto, Y., Nakagawa, T., & Shimizu, S.
- Affiliations
- Japan Science and Technology Agency (JP)
- Corresponding author
- Tsujimoto, Yoshihide
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 1757
- Issue
- 9-10
- Pages
- 1297-1300
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2015990527
- Cited by
- 188
- References
- 30
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 7 · 2021: 3 · 2020: 5 · 2019: 8 · 2018: 5 · 2017: 6 · 2016: 6 · 2015: 5 · 2014: 10 · 2013: 8 · 2012: 18
- FWCI
- 1.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health, Labour and Welfare
- 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 › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- mitochondrial permeability transition, mitochondrial permeability transition pore, cyclophilin D, voltage-dependent anion channel, adenine nucleotide translocase, apoptosis, necrosis, mitochondrial membrane permeability, mitochondrial membrane potential, mitochondrial swelling, Bcl-2, Bcl-xL, anti-apoptotic proteins, calcium homeostasis
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Animals, Necrosis, Permeability, Cell Death, Proto-Oncogene Proteins c-bcl-2, Cyclophilins, Mitochondrial Membranes
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
