Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death

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

Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria

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

Bax-induced Caspase Activation and Apoptosis via Cytochromec Release from Mitochondria Is Inhibitable by Bcl-xL

Finucane, 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

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

Necroptosis in Hepatosteatotic Ischaemia-Reperfusion Injury

Baidya, R., Crawford, D. H., Gautheron, J., Wang, H., & Bridle, K. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165931 · Cited by 41

Alkalization of cellular pH leads to cancer cell death by disrupting autophagy and mitochondrial function

Ying, C., Jin, C., Zeng, S., Chao, M., & Hu, X. (2022) · Oncogene · doi:10.1038/s41388-022-02396-6 · Cited by 35

Transient Metabolic Alkalosis During Early Reperfusion Abolishes Helium Preconditioning Against Myocardial Infarction: Restoration of Cardioprotection by Cyclosporin A in Rabbits

Pagel, P. S., & Krolikowski, J. G. (2009) · Anesthesia & Analgesia · doi:10.1213/ane.0b013e318193e934 · Cited by 35

Chronic ethanol consumption enhances sensitivity to Ca2+-mediated opening of the mitochondrial permeability transition pore and increases cyclophilin D in liver

King, A. L., Swain, T. M., Dickinson, D. A., Lesort, M. J., & Bailey, S. M. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00246.2010 · Cited by 36

The mitochondrial permeability transition pore as a target of cardioprotective signaling

Baines, C. P. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00575.2007 · Cited by 35

Vacuolar functions determine the mode of cell death

Schauer, A., Knauer, H., Ruckenstuhl, C., Fussi, H., Durchschlag, M., Potocnik, U., & Fröhlich, K. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.11.006 · Cited by 35

Caspase‐dependent alteration of the ADP/ATP translocator triggers the mitochondrial permeability transition which is not required for the low‐potassium‐dependent apoptosis of cerebellar granule cells

Atlante, A., Bobba, A., Lidia de, B. A. R. I., Fontana, F., Calissano, P., Marra, E., & Passarella, S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03820.x · Cited by 36

Fighting cancer by triggering non-canonical mitochondrial permeability transition-driven necrosis through reactive oxygen species induction

Xiao, Q., Zhong, B., Hou, Y., Wang, M., Guo, B., Lin, L., Zhou, Y., & Chen, X. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.03.020 · Cited by 34

Hematopoietic stem cells: Understanding the mechanisms to unleash the therapeutic potential of hematopoietic stem cell transplantation

Aljagthmi, A. A., & Abdel‐Aziz, A. K. (2025) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04126-z · Cited by 43

Cyclosporin A Promotes Tumor Angiogenesis in a Calcineurin-Independent Manner by Increasing Mitochondrial Reactive Oxygen Species

Zhou, A. Y., & Ryeom, S. W. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0136 · Cited by 35

Elovl6 regulates mechanical damage-induced keratinocyte death and skin inflammation

Nakamura, Y., Matsuzaka, T., Tahara‐Hanaoka, S., Shibuya, K., Shimano, H., Nakahashi-Oda, C., & Shibuya, A. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1226-1 · Cited by 34

Sirtuin 3 deficiency exacerbates age‐related periodontal disease

Chen, J., Zhang, Y., Gao, J., Li, T., Gan, X., & Yu, H. (2021) · Journal of Periodontal Research · doi:10.1111/jre.12930 · Cited by 36

ANT2 drives proinflammatory macrophage activation in obesity

Moon, J.-S., da Cunha, F. F., Huh, J. Y., Andreyev, A. Y., Lee, J., Mahata, S. K., Reis, F. C. G., Nasamran, C. A., & Lee, Y. S. (2021) · JCI Insight · doi:10.1172/jci.insight.147033 · Cited by 36

Having a swell time – mitochondrial morphology and plant cell death programmes

Logan, D. C. (2008) · Journal of Microscopy · doi:10.1111/j.1365-2818.2008.02037.x · Cited by 33

Mitochondrial Ca2+ transport and permeability transition in zebrafish (Danio rerio)

Azzolin, L., Basso, E., Argenton, F., & Bernardi, P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.07.002 · Cited by 34

Physiological Consequences of Programmed Necrosis, an Alternative form of Cell Demise

Cho, Y. S., Park, S. Y., Shin, H., & Chan, F. K.-M. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0066-3 · Cited by 33

CKMT1 regulates the mitochondrial permeability transition pore in a process that provides evidence for alternative forms of the complex

Datler, C., Pazarentzos, E., Mahul‐Mellier, A., Chaisaklert, W., Hwang, M., Osborne, F. N., & Grimm, S. (2014) · Journal of Cell Science · doi:10.1242/jcs.140467 · Cited by 33

Complex Contribution of Cyclophilin D to Ca2+-induced Permeability Transition in Brain Mitochondria, with Relation to the Bioenergetic State

Dóczi, J., Turiák, L., Vajda, S., Mándi, M., Törőcsik, B., Gerencser, A. A., Kiss, G., Konràd, C., Ádám‐Vizi, V., & Chinopoulos, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.196600 · Cited by 35

Modulation of the mitochondrial permeability transition by cyclophilin D: Moving closer to F0–F1 ATP synthase?

Chinopoulos, C., & Ádám‐Vizi, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.007 · Cited by 32

Changes in mitochondrial membrane potential and reactive oxygen species during wogonin‐induced cell death in human hepatoma cells

Yu, J. Q., Liu, H. B., Tian, D. Z., Liu, Y. W., Lei, J. C., & Zou, G. L. (2007) · Hepatology Research · doi:10.1111/j.1872-034x.2007.00003.x · Cited by 33

Is p53 the Long-Sought Molecular Trigger for Cyclophilin D–Regulated Mitochondrial Permeability Transition Pore Formation and Necrosis?

Karch, J. M., & Molkentin, J. D. (2012) · Circulation Research · doi:10.1161/circresaha.112.280990 · Cited by 33

Mitochondrial electron transport chain complex III sustains hepatitis E virus replication and represents an antiviral target

Qu, C., Zhang, S., Wang, W., Li, M., Wang, Y., van der Heide‐Mulder, M., Shokrollahi, E., Hakim, M. S., Raat, N. J. H., Peppelenbosch, M. P., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800620r · Cited by 33

A computationally designed binding mode flip leads to a novel class of potent tri-vector cyclophilin inhibitors

Simone, A. D., Georgiou, C., Ioannidis, H., Gupta, A. A., Juárez‐Jiménez, J., Doughty-Shenton, D., Blackburn, E. A., Wear, M. A., Richards, J. P., Barlow, P. N., et al. (2018) · Chemical Science · doi:10.1039/c8sc03831g · Cited by 33

Quercetin induced ROS production triggers mitochondrial cell death of human embryonic stem cells

Kim, S.-Y., Jeong, H., Hong, S.-K., Lee, M., Cho, S.-J., & Cha, H. (2016) · Oncotarget · doi:10.18632/oncotarget.11070 · Cited by 33

Geldanamycin, an Inhibitor of Hsp90, Potentiates Cytochrome P4502E1-Mediated Toxicity in HepG2 Cells

Dey, A., & Cederbaum, A. I. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.101808 · Cited by 32

Mastoparan peptide causes mitochondrial permeability transition not by interacting with specific membrane proteins but by interacting with the phospholipid phase

Yamamoto, T., Ito, M., Kageyama, K., Kuwahara, K., Yamashita, K., Takiguchi, Y., Kitamura, S., Terada, H., & Shinohara, Y. (2014) · FEBS Journal · doi:10.1111/febs.12930 · Cited by 31

Cyclophilin D regulates mitochondrial flashes and metabolism in cardiac myocytes

Shang, W. H., Gao, H., Lu, F., Ma, Q., Fang, H., Sun, T., Xu, J., Ding, Y., Lin, Y., Wang, Y., et al. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.10.036 · Cited by 31

An apoptosis signal‐regulating kinase 1 inhibitor reduces cardiomyocyte apoptosis and infarct size in a rat ischemia‐reperfusion model

Gerczuk, P., Breckenridge, D., Liles, J., Budas, G., Shryock, J., Belardinelli, L., Kloner, R. A., & Dai, W. (2012) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e31825ea0fa · Cited by 33

Delayed-onset caspase-dependent massive hepatocyte apoptosis upon fas activation in bak/bax-deficient mice

Hikita, H., Takehara, T., Kodama, T., Shimizu, S., Shigekawa, M., Hosui, A., Miyagi, T., Tatsumi, T., Ishida, H., Li, W., et al. (2011) · Hepatology · doi:10.1002/hep.24305 · Cited by 32

Prostate cancer regulatory networks

Altieri, D. C., Languino, L. R., Lian, J. B., Stein, J. L., Leav, I., van Wijnen, A. J., Jiang, Z., & Stein, G. S. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22162 · Cited by 33

An Analogue of Resveratrol HS-1793 Exhibits Anticancer Activity Against MCF-7 Cells Via Inhibition of Mitochondrial Biogenesis Gene Expression

Jeong, S. H., Song, I. S., Kim, H. K., Lee, S. R., Song, S., Suh, H., Yoon, Y. G., Yoo, Y. H., Kim, N., Rhee, B. D., et al. (2012) · Molecules and Cells · doi:10.1007/s10059-012-0081-7 · Cited by 32

Cyclosporine Inhibits Mouse Cytomegalovirus Infection via a Cyclophilin-Dependent Pathway Specifically in Neural Stem/Progenitor Cells

Kawasaki, H., Mocarski, E. S., Kosugi, I., & Tsutsui, Y. (2007) · Journal of Virology · doi:10.1128/jvi.00261-07 · Cited by 31

Mitochondrial calcium uptake capacity as a therapeutic target in the R6/2 mouse model of Huntington's disease

Perry, G. M., Tallaksen‐Greene, S. J., Kumar, A., Heng, M. Y., Kneynsberg, A., van Groen, T., Detloff, P. J., Albin, R. L., & Lesort, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq247 · Cited by 33

Therapeutic Potential of a Novel Necrosis Inhibitor, 7-Amino-Indole, in Myocardial Ischemia–Reperfusion Injury

Hwang, I., Kim, J., Kim, J.-H., Lee, J., Seo, J.-Y., Lee, J., Park, J., Yang, H., Kim, S.-H., Cho, H., et al. (2018) · Hypertension · doi:10.1161/hypertensionaha.117.09405 · Cited by 30

The role of RIP3 in cardiomyocyte necrosis induced by mitochondrial damage of myocardial ischemia–reperfusion

Hou, H., Wang, Y., Li, Q., Li, Z., Teng, Y., Li, J., Wang, X., Chen, J., & Huang, N. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmy108 · Cited by 31

Oligomycin-induced proton uncoupling

Hearne, A., Chen, H., Monarchino, A., & Wiseman, J. S. (2020) · Toxicology in Vitro · doi:10.1016/j.tiv.2020.104907 · Cited by 39

The Isopeptidase Inhibitor G5 Triggers a Caspase-independent Necrotic Death in Cells Resistant to Apoptosis

Fontanini, A., Foti, C., Potu, H., Crivellato, E., Maestro, R., Bernardi, P., Demarchi, F., & Brancolini, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806113200 · Cited by 31

The targeting of cyclophilin D by RNAi as a novel cardioprotective therapy: evidence from two-photon imaging

Kato, M., Akao, M., Matsumoto-Ida, M., Makiyama, T., Iguchi, M., Takeda, T., Shimizu, S., & Kita, T. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp094 · Cited by 31

Insulin receptor substrate-1 prevents autophagy-dependent cell death caused by oxidative stress in mouse NIH/3T3 cells

Chan, S. H., Kikkawa, U., Matsuzaki, H., Chen, J.-H., & Chang, W. (2012) · Journal of Biomedical Science · doi:10.1186/1423-0127-19-64 · Cited by 31

Ontogenetic development of cardiac tolerance to oxygen deprivation – possible mechanisms

Ošťádal, B., Ošťádalová, I., Kolář, F., Charvátová, Z., & Netuka, I. (2009) · Physiological Research · doi:10.33549/physiolres.931920 · Cited by 31

Key hepatoprotective roles of mitochondria in liver regeneration

Lamanilao, G. G., Doğan, M., Patel, P. S., Azim, S., Patel, D. S., Bhattacharya, S. K., Eason, J. D., Kuscu, C., Kuscu, C., & Bajwa, A. (2023) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00220.2022 · Cited by 30

Identification of a novel compound that inhibits both mitochondria-mediated necrosis and apoptosis

Arakawa, S., Nakanomyo, I., Kudo-Sakamoto, Y., Akazawa, H., Komuro, I., & Shimizu, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.022 · Cited by 30

Paracrine effects of hypoxic fibroblast-derived factors on the MPT-ROS threshold and viability of adult rat cardiac myocytes

Shivakumar, K., Sollott, S. J., Sangeetha, M., Subrayan, S., Ziman, B. D., Wang, S., & Lakatta, E. G. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.91443.2007 · Cited by 30

Cardioprotection by Noble Gases

Pagel, P. S. (2009) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2009.03.016 · Cited by 30

The Role of Macrophages During Zebrafish Injury and Tissue Regeneration Under Infectious and Non-Infectious Conditions

Bohaud, C., Johansen, M. D., Jørgensen, C., Ipseiz, N., Kremer, L., & Djouad, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.707824 · Cited by 31

From Apoptosis to Necroptosis: The Death Wishes to Cancer

Meng, X., Dang, T., & Chai, J. (2021) · Cancer Control · doi:10.1177/10732748211066311 · Cited by 32

Neuroprotective efficacy of FR901459, a novel derivative of cyclosporin A, in in vitro mitochondrial damage and in vivo transient cerebral ischemia models

Muramatsu, Y., Furuichi, Y., Tojo, N., Moriguchi, A., Maemoto, T., Nakada, H., Hino, M., & Matsuoka, N. (2007) · Brain Research · doi:10.1016/j.brainres.2007.02.036 · Cited by 30

Evaluation of putative inhibitors of mitochondrial permeability transition for brain disorders — Specificity vs. toxicity

Morota, S., Månsson, R., Hansson, M. J., Kasuya, K., Shimazu, M., Hasegawa, E., Yanagi, S., Omi, A., Uchino, H., & Elmér, E. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.036 · Cited by 31

Therapeutic implications of down-regulation of cyclophilin D in bipolar disorder

Kubota, M., Kasahara, T., Iwamoto, K., Komori, A., Ishiwata, M., Miyauchi, T., & Kato, T. (2010) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145710000362 · Cited by 30

From the Ca 2+ -activated F 1 F O -ATPase to the mitochondrial permeability transition pore: an overview

Nesci, S., Trombetti, F., Ventrella, V., & Pagliarani, A. (2018) · Biochimie · doi:10.1016/j.biochi.2018.06.022 · Cited by 31

Therapeutic peptides: Targeting the mitochondrion to modulate apoptosis

Jacotot, E. D., Deniaud, A., Borgne‐Sanchez, A., Touat-Hamici, Z., Briand, J., Bras, M. L., & Brenner, C. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.07.002 · Cited by 30

Multiple Cell Death Programs Contribute to Myocardial Infarction

Jia, X. F., Liang, F. G., & Kitsis, R. N. (2021) · Circulation Research · doi:10.1161/circresaha.121.319584 · Cited by 30

Alpha Particle–Emitting Radiopharmaceuticals as Cancer Therapy: Biological Basis, Current Status, and Future Outlook for Therapeutics Discovery

Coll, R. P., Bright, S. J., Martinus, D. K. J., Georgiou, D. K., Sawakuchi, G. O., & Manning, H. C. (2023) · Molecular Imaging and Biology · doi:10.1007/s11307-023-01857-y · Cited by 30

Serine Hydrolase Inhibitors Block Necrotic Cell Death by Preventing Calcium Overload of the Mitochondria and Permeability Transition Pore Formation

Yun, B., Lee, H.-J., Ghosh, M., Cravatt, B. F., Hsu, K., Bonventre, J. V., Ewing, H., Gelb, M. H., & Leslie, C. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497651 · Cited by 29

Targeting Cell Death

Hausenloy, D. J., & Scorrano, L. (2007) · Clinical Pharmacology & Therapeutics · doi:10.1038/sj.clpt.6100352 · Cited by 30

Role of apoptosis repressor with caspase recruitment domain (ARC) in cell death and cardiovascular disease

Zhang, J., Zheng, X., Wang, P., Wang, J., & Ding, W. (2021) · APOPTOSIS · doi:10.1007/s10495-020-01653-x · Cited by 29

Non-energy mechanism of phosphocreatine on the protection of cell survival

Liu, W., Qaed, E., Zhu, H. G., Dong, M. X., & Tang, Z. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111839 · Cited by 32

The molecular mosaic of regulated cell death in the cardiovascular system

Martens, M. D., Karch, J. M., & Gordon, J. W. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166297 · Cited by 31

Cyclophilin and viruses: cyclophilin as a cofactor for viral infection and possible anti-viral target.

Watashi, K., & Shimotohno, K. (2007) · Europe PMC (PubMed Central) · Cited by 29

Alternative Cell Death Pathways and Cell Metabolism

Fulda, S. (2013) · International Journal of Cell Biology · doi:10.1155/2013/463637 · Cited by 29

Insensitivity to glutamate neurotoxicity mediated by NMDA receptors in association with delayed mitochondrial membrane potential disruption in cultured rat cortical neurons

Kambe, Y., Nakamichi, N., Георгиев, Д., Nakamura, N., Taniura, H., & Yoneda, Y. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05270.x · Cited by 29

Pharmacological inhibition of mitochondrial membrane permeabilization for neuroprotection

Hisatomi, T., Ishibashi, T., Miller, J. W., & Kroemer, G. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.007 · Cited by 29

The meaning of different forms of structural myocardial injury, immune response and timing of infarct necrosis and cardiac repair.

Turillazzi, E., Pomara, C., Bello, S., Neri, M., Riezzo, I., & Fineschi, V. (2015) · Current Vascular Pharmacology · doi:10.2174/15701611113119990008 · Cited by 28

Pharmacologic Targeting or Genetic Deletion of Mitochondrial Cyclophilin D Protects from NSAID-Induced Small Intestinal Ulceration in Mice

LoGuidice, A., Ramírez‐Alcántara, V., Proli, A. J., Gavillet, B., & Boelsterli, U. A. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq226 · Cited by 28

Post-Injury Treatment with NIM811 Promotes Recovery of Function in Adult Female Rats after Spinal Cord Contusion: A Dose-Response Study

Springer, J. E., Visavadiya, N. P., Sullivan, P. G., & Hall, E. D. (2017) · Journal of Neurotrauma · doi:10.1089/neu.2017.5167 · Cited by 29

CypD-mPTP axis regulates mitochondrial functions contributing to osteogenic dysfunction of MC3T3-E1 cells in inflammation

Gan, X., Zhang, L., Liu, B., Zhu, Z., He, Y., Chen, J., Zhu, J., & Yu, H. (2018) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-018-0627-z · Cited by 28

Aged kidney: can we protect it? Autophagy, mitochondria and mechanisms of ischemic preconditioning

Jankauskas, S. S., Silachev, D. N., Andrianova, N. V., Pevzner, I. B., Zorova, L. D., Popkov, V. A., Plotnikov, E. Y., & Zorov, D. B. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1482149 · Cited by 28

Selective protection of human cardiomyocytes from anthracycline cardiotoxicity by small molecule inhibitors of MAP4K4

Golforoush, P. A., Narasimhan, P., Cháves, P., Lawrence, E., Newton, G. K., Yan, R., Harding, S. E., Perrior, T. R., Chapman, K. L., & Schneider, M. D. (2020) · Scientific Reports · doi:10.1038/s41598-020-68907-1 · Cited by 28

Post‐conditioning with cyclosporine A fails to reduce the infarct size in an in vivo porcine model

Lie, R. H., Stoettrup, N. B., Sloth, E., Hasenkam, J. M., KROYER, R., & Nielsen, T. T. (2010) · Acta Anaesthesiologica Scandinavica · doi:10.1111/j.1399-6576.2010.02241.x · Cited by 28

Cell death, dysglycemia and myocardial infarction

TIAN, X.-F., Cui, M., Yang, S., ZHOU, Y.-J., & Hu, D. (2013) · Biomedical Reports · doi:10.3892/br.2013.67 · Cited by 27

Direct toxic effects of aqueous extract of cigarette smoke on cardiac myocytes at clinically relevant concentrations

Yamada, S., Zhang, X. Q., Kadono, T., Matsuoka, N., Rollins, D. E., Badger, T. J., Rodesch, C. K., & Barry, W. H. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.01.008 · Cited by 28

The therapeutic potential of mitochondrial channels in cancer, ischemia–reperfusion injury, and neurodegeneration

Peixoto, P. M. V., Dejean, L. M., & Kinnally, K. W. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.03.003 · Cited by 29

Necrotic cell death: From reversible mitochondrial uncoupling to irreversible lysosomal permeabilization

Giusti, C., Luciani, M., Klein, G., Aubry, L., Tresse, E., Kosta, A., & Golstein, P. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.09.028 · Cited by 30

Pharmacological approaches to reperfusion therapy

Morel, O., Perret, T., Delarche, N., Labeque, J.-N., Jouve, B., Elbaz, M., Piot, C. A., & Ovize, M. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs114 · Cited by 28

Inhibition of the mitochondrial permeability transition improves bone fracture repair

Shares, B. H., Smith, C. O., Sheu, T., Sautchuk, R., Schilling, K. J., Shum, L. C., Paine, A., Huber, A., Gira, E., Brown, E. B., et al. (2020) · Bone · doi:10.1016/j.bone.2020.115391 · Cited by 28

Mitochondrial aldehyde dehydrogenase 2 activation and cardioprotection

Gong, D., Zhang, H., & Hu, S. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.03.017 · Cited by 28

Gene expression profiles of necrosis and apoptosis induced by 5-fluoro-2′-deoxyuridine

Sato, A., Hiramoto, A., Uchikubo, Y., Miyazaki, E., Satake, A., Naito, T., Hiraoka, O., Miyake, T., Kim, H., & Wataya, Y. (2008) · Genomics · doi:10.1016/j.ygeno.2008.02.002 · Cited by 28

Mechanisms Underlying Dichotomous Procoagulant COAT Platelet Generation—A Conceptual Review Summarizing Current Knowledge

Veuthey, L., Aliotta, A., Calderara, D. B., Portela, C. P., & Alberio, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052536 · Cited by 27

Mitochondrial sirtuin 3 and role of natural compounds: the effect of post-translational modifications on cellular metabolism

Oppedisano, F., Nesci, S., & Spagnoletta, A. (2024) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2024.2377094 · Cited by 29

Investigating the Mitochondrial Permeability Transition Pore in Disease Phenotypes and Drug Screening

Bhosale, G., & Duchen, M. R. (2019) · Current Protocols in Pharmacology · doi:10.1002/cpph.59 · Cited by 28

Sirtuin 3 and mitochondrial permeability transition pore (mPTP): A systematic review

Yang, Y., Wang, W., Tian, Y., & Shi, J. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.03.004 · Cited by 27

Nelfinavir Inhibits Intra-Mitochondrial Calcium Influx and Protects Brain against Hypoxic-Ischemic Injury in Neonatal Mice

Utkina-Sosunova, I. V., Niatsetskaya, Z. V., Sosunov, S. A., Ratner, V. I., Matsiukevich, D., & Ten, V. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062448 · Cited by 27

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

Effect of magnesium on calcium‐induced depolarisation of mitochondrial transmembrane potential

Račay, P. (2007) · Cell Biology International · doi:10.1016/j.cellbi.2007.08.024 · Cited by 26

Computational Insights on the Competing Effects of Nitric Oxide in Regulating Apoptosis

Bagci, E. Z., Yoram Vodovotz, B., Billiar, T. R., Ermentrout, B., & Bahar, İ. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002249 · Cited by 28

Interactions of GSK-3 With Mitochondrial Permeability Transition Pore Modulators During Preconditioning: Age-Associated Differences

Zhu, J., Rebecchi, M. J., Glass, P. S. A., Brink, P. R., & Liu, L. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/gls205 · Cited by 27

Regulator of Calcineurin 1-1L Protects Cardiomyocytes Against Hypoxia-induced Apoptosis via Mitophagy

Yan, L., Yang, H., Li, Y., Duan, H., Wu, J., Qian, P., Li, B., & Wang, S. (2014) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000121 · Cited by 26

AICAR induces AMPK-independent programmed necrosis in prostate cancer cells

Guo, F., Liu, S., Gao, X.-H., & Zhang, L. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.077 · Cited by 27

Cyclophilin D Is Involved in the Regulation of Autophagy and Affects the Lifespan of P. anserina in Response to Mitochondrial Oxidative Stress

Kramer, P., Jung, A. T., Hamann, A., & Osiewacz, H. D. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00165 · Cited by 27

A homolog of cyclophilin D is expressed in Trypanosoma cruzi and is involved in the oxidative stress–damage response

Bustos, P. L., Volta, B. J., Perrone, A. E., Milduberger, N., & Búa, J. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.92 · Cited by 25

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

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

Roles of Vpr and Vpx in modulating the virus-host cell relationship

Planelles, V., & Barker, E. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.05.002 · Cited by 26

The Importance of Humanized Yeast to Better Understand the Role of Bcl-2 Family in Apoptosis: Finding of Novel Therapeutic Opportunities

Silva, R. D., Manon, S., Gonçalves, J., Saraiva, L., & Côrte‐Real, M. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211795049651 · Cited by 27

Mitochondrial drug targets in neurodegenerative diseases

Lee, J. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.11.032 · Cited by 26

Glucosylceramide synthase regulates the proliferation and apoptosis of liver cells in vitro by Bcl-2/Bax pathway

Li, J., Zheng, S.-J., Wang, L., Liu, S., Ren, F., Chen, Y., Bai, L., Liu, M., & Duan, Z. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7580 · Cited by 26

SR-Mitochondria Crosstalk Shapes Ca Signalling to Impact Pathophenotype in Disease Models Marked by Dysregulated Intracellular Ca Release

Tow, B. D., Deb, A., Neupane, S., Patel, S. M., Reed, M., Loper, A.-B., Eliseev, R. A., Knollmann, B. C., Györke, S., & Liu, B. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab324 · Cited by 27

Mechanisms of non-apoptotic programmed cell death in diabetes and heart failure

Dorn, G. W. (2010) · Cell Cycle · doi:10.4161/cc.9.17.12944 · Cited by 26

Cyclophilin‐D: a resident regulator of mitochondrial gene expression

Radhakrishnan, J., Bazarek, S. F., Chandran, B., & Gazmuri, R. J. (2015) · The FASEB Journal · doi:10.1096/fj.14-263855 · Cited by 25

Effects of permeability transition inhibition and decrease in cytochrome c content on doxorubicin toxicity in K562 cells

Oliveira, F. D., Chauvin, C., Ronot, X., Mousseau, M., Leverve, X. M., & Fontaine, E. M. (2005) · Oncogene · doi:10.1038/sj.onc.1209293 · Cited by 27

Pharmacological screening and enzymatic assays for apoptosis

Belzacq, A.-S. (2009) · Frontiers in bioscience · doi:10.2741/3470 · Cited by 29

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

Role of the mitochondrial membrane permeability transition in cell death

Tsujimoto, Y., & Shimizu, S. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0525-7 · Cited by 570

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

Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis

Li, Y., Johnson, N., Capano, M., Edwards, M., & Crompton, M. (2004) · Biochemical Journal · doi:10.1042/bj20040669 · Cited by 165

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