Mitochondrial apoptosis without VDAC

Mitochondrial membrane permeabilization in cell death

Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works

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

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 · see citing works

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

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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 · see citing works

Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels

Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · 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

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 · see citing works

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 · see citing works

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 · see citing works

Bcl-xL Prevents Cell Death following Growth Factor Withdrawal by Facilitating Mitochondrial ATP/ADP Exchange

Heiden, M. G. V., Chandel, N. S., Schumacker, P. T., & Thompson, C. B. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80307-x · Cited by 505 · see citing works

Bid, but Not Bax, Regulates VDAC Channels

Rostovtseva, T. K., Antonsson, B. E., Suzuki, M., Youle, R. J., Colombini, M., & Bezrukov, S. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310593200 · Cited by 197 · see citing works

TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax

Bellot, G., Cartron, P., Er, E., Oliver, L., Juin, P. P., Armstrong, L. C., BORNSTEIN, P. K., Mihara, K., Manon, S., & Vallette, F. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402055 · Cited by 156 · see citing works

Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA

Poncet, D., Pauleau, A., Szabadkai, G., Vozza, A., Scholz, S. R., Bras, M. L., Brière, J.-J., Jalil, A., Moigne, R. L., Brenner, C., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604069 · Cited by 100 · see citing works

Localization of the voltage-dependent anion channel-1 Ca2+-binding sites

Israelson, A., Abu‐Hamad, S., Zaid, H., Nahon, E., & Shoshan‐Barmatz, V. (2006) · Cell Calcium · doi:10.1016/j.ceca.2006.06.005 · Cited by 79 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

The Role of Mitochondria in Apoptosis

Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987 · see citing works

Targeting mitochondria for cancer therapy

Fulda, S., Galluzzi, L., & Kroemer, G. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3137 · Cited by 1,638 · see citing works

Essential versus accessory aspects of cell death: recommendations of the NCCD 2015

Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · see citing works

VDAC, a multi-functional mitochondrial protein regulating cell life and death

Shoshan‐Barmatz, V., Pinto, V. D., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 792 · see citing works

Metabolic control of cell death

Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 661 · see citing works

Mitochondrial Control of Cellular Life, Stress, and Death

Galluzzi, L., Kepp, O., Trojel‐Hansen, C., & Kroemer, G. (2012) · Circulation Research · doi:10.1161/circresaha.112.268946 · Cited by 545 · see citing works

Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition

Bonora, M., Bononi, A., Marchi, E. D., Giorgi, C., Lebiedzińska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 454 · see citing works

Viral Control of Mitochondrial Apoptosis

Galluzzi, L., Brenner, C., Morselli, E., Touat-Hamici, Z., & Kroemer, G. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000018 · Cited by 423 · see citing works

Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration

Rostovtseva, T. K., Sheldon, K. L., Hassanzadeh, E., Monge, C., Saks, V. A., Bezrukov, S. M., & Sackett, D. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806303105 · Cited by 366 · see citing works

Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition

Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330 · see citing works

The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor

Rong, Y.-P., Bultynck, G., Aromolaran, A. S., Zhong, F., Parys, J. B., SMEDT, H. D., Mignery, G. A., Roderick, H. L., Bootman, M. D., & Distelhorst, C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907555106 · Cited by 306 · see citing works

Mitochondrial gateways to cancer

Galluzzi, L., Morselli, E., Kepp, O., Vitale, I., Rigoni, A., Vacchelli, E., Michaud, M., Zischka, H., Castedo, M., & Kroemer, G. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.08.002 · Cited by 296 · see citing works

Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles

Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 299 · see citing works

Oligomerization of the Mitochondrial Protein Voltage-Dependent Anion Channel Is Coupled to the Induction of Apoptosis

Keinan, N., Tyomkin, D., & Shoshan‐Barmatz, V. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00165-10 · Cited by 269 · see citing works

Molecular mechanisms of regulated necrosis

Galluzzi, L., Kepp, O., Krautwald, S., Kroemer, G., & Linkermann, A. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.02.006 · Cited by 258 · see citing works

No death without life: vital functions of apoptotic effectors

Galluzzi, L., Joza, N. A., Tasdemir, E., Maiuri, M. C., Hengartner, M. O., Abrams, J., Tavernarakis, N., Penninger, J. M., Madeo, F., & Kroemer, G. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.28 · Cited by 256 · see citing works

Intracellular Ca2+ signaling and Ca2+ microdomains in the control of cell survival, apoptosis and autophagy

Rovere, R. M. L. L., Roest, G., Bultynck, G., & Parys, J. B. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.04.005 · Cited by 256 · see citing works

Multifunctional roles of gelsolin in health and diseases

Li, G. H., Arora, P. D., Chen, Y., McCulloch, C. A., & Liu, P. J. (2010) · Medicinal Research Reviews · doi:10.1002/med.20231 · Cited by 255 · see citing works

VDAC, a multi-functional mitochondrial protein as a pharmacological target

Shoshan‐Barmatz, V., & Ben-Hail, D. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.001 · Cited by 250 · see citing works

The mitochondrial voltage-dependent anion channel 1 in tumor cells

Shoshan‐Barmatz, V., Ben-Hail, D., Admoni, L., Krelin, Y., & Tripathi, S. S. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.040 · Cited by 245 · see citing works

VDAC regulation: role of cytosolic proteins and mitochondrial lipids

Rostovtseva, T. K., & Bezrukov, S. M. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9145-y · Cited by 220 · see citing works

Hierarchical involvement of Bak, VDAC1 and Bax in cisplatin-induced cell death

Tajeddine, N., Galluzzi, L., Kepp, O., Hangen, E., Morselli, E., Senovilla, L., Araujo, N., Pinna, G., Larochette, N., Zamzami, N., et al. (2008) · Oncogene · doi:10.1038/onc.2008.63 · Cited by 207 · see citing works

VDAC1: from structure to cancer therapy

Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 193 · see citing works

New Insights into the Mechanisms for Photodynamic Therapy-Induced Cancer Cell Death

Yoo, J., & Ha, K. (2012) · International review of cytology · doi:10.1016/b978-0-12-394306-4.00010-1 · Cited by 174 · see citing works

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

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

Staying alive: bacterial inhibition of apoptosis during infection

Faherty, C. S., & Maurelli, A. T. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.02.001 · Cited by 154 · see citing works

Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization: release of cytochrome c, AIF and Smac/Diablo

Shoshan‐Barmatz, V., Keinan, N., Abu‐Hamad, S., Tyomkin, D., & Aram, L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.003 · Cited by 147 · see citing works

Redox Control of Protein Kinase C: Cell- and Disease-Specific Aspects

Giorgi, C., Agnoletto, C., Baldini, C., Bononi, A., Bonora, M., Marchi, S., Missiroli, S., Patergnani, S., Poletti, F., Rimessi, A., et al. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2825 · Cited by 150 · see citing works

Mitochondrial VDAC1: Function in Cell Life and Death and a Target for Cancer Therapy

Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 139 · see citing works

The Identity and Regulation of the Mitochondrial Permeability Transition Pore

Juhaszova, M., Wang, S., Zorov, D. B., Nuss, H. B., Gleichmann, M., Mattson, M. P., & Sollott, S. J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1420.023 · Cited by 138 · see citing works

Bad Targets the Permeability Transition Pore Independent of Bax or Bak to Switch between Ca2+-Dependent Cell Survival and Death

Roy, S. S., Madesh, M., Davies, E., Antonsson, B. E., Danial, N. N., & Hajnóczky, G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.018 · Cited by 138 · see citing works

Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics

Shoshan‐Barmatz, V., Krelin, Y., Shteinfer‐Kuzmine, A., & Arif, T. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00154 · Cited by 134 · see citing works

The Mitochondrial Voltage-Dependent Anion Channel 1, Ca2+ Transport, Apoptosis, and Their Regulation

Shoshan‐Barmatz, V., De, S., & Meir, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00060 · Cited by 122 · see citing works

Bax: Addressed to kill

Renault, T. T., & Manon, S. (2011) · Biochimie · doi:10.1016/j.biochi.2011.05.013 · Cited by 119 · see citing works

Targeting post-mitochondrial effectors of apoptosis for neuroprotection

Galluzzi, L., Morselli, E., Kepp, O., & Kroemer, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.09.006 · Cited by 119 · see citing works

MicroRNA-519a-3p mediates apoptosis resistance in breast cancer cells and their escape from recognition by natural killer cells

Breunig, C., Pahl, J. H. W., Kueblbeck, M., Miller, M., Antonelli, D., Erdem, N., Wirth, C., Will, R. D., Bott, A., Cerwenka, A., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.364 · Cited by 121 · see citing works

Mitochondrial function and abnormalities implicated in the pathogenesis of ASD

Castora, F. J. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.12.015 · Cited by 104 · see citing works

Induction of heat shock protein 70 inhibits ischemic renal injury

Wang, Z., Gall, J. M., Bonegio, R. G. B., Havasi, A., Hunt, C. R., Sherman, M. Y., Schwartz, J. H., & Borkan, S. C. (2011) · Kidney International · doi:10.1038/ki.2010.527 · Cited by 97 · see citing works

Mechanisms of Cdc48/VCP-mediated cell death — from yeast apoptosis to human disease

Braun, R. J., & Zischka, H. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.015 · Cited by 98 · see citing works

The optic nerve: A “mito-window” on mitochondrial neurodegeneration

Maresca, A., Morgia, C. L., Caporali, L., Valentino, M. L., & Carelli, V. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.08.004 · Cited by 92 · see citing works

Functions of BCL-X L at the Interface between Cell Death and Metabolism

Michels, J., Kepp, O., Senovilla, L., Lissa, D., Castedo, M., Kroemer, G., & Galluzzi, L. (2013) · International Journal of Cell Biology · doi:10.1155/2013/705294 · Cited by 92 · see citing works

Reactive oxygen species accumulation contributes to gambogic acid-induced apoptosis in human hepatoma SMMC-7721 cells

Nie, F.-F., Zhang, X., Qi, Q., Yang, L., Yang, Y., Liu, W., Lu, N., Wu, Z., You, Q., & Guo, Q. (2009) · Toxicology · doi:10.1016/j.tox.2009.03.010 · Cited by 90 · see citing works

Expression of a Truncated Active Form of VDAC1 in Lung Cancer Associates with Hypoxic Cell Survival and Correlates with Progression to Chemotherapy Resistance

Brahimi-Horn, M. C., Ben-Hail, D., Ilié, M., Gounon, P., Rouleau, M., Hofman, V., Doyen, J., Mari, B. P., Shoshan‐Barmatz, V., Hofman, P. M., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3940 · Cited by 80 · see citing works

New insights into mitochondrial structure during cell death

Perkins, G. A., Bossy‐Wetzel, E., & Ellisman, M. H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.021 · Cited by 76 · see citing works

Efficient Elimination of Cancer Cells by Deoxyglucose-ABT-263/737 Combination Therapy

Yamaguchi, R., Janssen, E. M., Perkins, G. A., Ellisman, M. H., Kitada, S., & Reed, J. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024102 · Cited by 73 · see citing works

VDAC phosphorylation, a lipid sensor influencing the cell fate

Martel, C., Wang, Z., & Brenner, C. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.07.009 · Cited by 69 · see citing works

Regulation of calcium homeostasis in endoplasmic reticulum-mitochondria crosstalk: Implications for skeletal muscle atrophy

Li, X., Zhao, X., Qin, Z., Li, J., Sun, B., & Liu, L. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-024-02014-w · Cited by 69 · see citing works

Dynamics of mitochondrial structure during apoptosis and the enigma of Opa1

Yamaguchi, R., & Perkins, G. A. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.005 · Cited by 63 · see citing works

Antitumor mechanisms of an exopolysaccharide from Lactobacillus fermentum on HT-29 cells and HT-29 tumor-bearing mice

Li, F., Jiao, X., Zhao, J., Liao, X., Wei, Y., & Li, Q. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.04.023 · Cited by 60 · see citing works

Gelsolin regulates proliferation, apoptosis, migration and invasion in human oral carcinoma cells

Deng, R., Hao, J., Han, W., Ni, Y., Huang, X., & Hu, Q. (2015) · Oncology Letters · doi:10.3892/ol.2015.3002 · Cited by 52 · see citing works

Mitochondrial membrane cholesterol, the voltage dependent anion channel (VDAC), and the Warburg effect

Campbell, A. M., & Chan, S. H. P. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9138-x · Cited by 52 · see citing works

How long noncoding RNAs enforce their will on mitochondrial activity: regulation of mitochondrial respiration, reactive oxygen species production, apoptosis, and metabolic reprogramming in cancer

Paepe, B. D., Lefever, S., & Mestdagh, P. (2017) · Current Genetics · doi:10.1007/s00294-017-0744-1 · Cited by 51 · see citing works

Role of calcium and cyclophilin D in the regulation of mitochondrial permeabilization induced by glutathione depletion

Lü, C., & Armstrong, J. S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.196 · Cited by 50 · see citing works

Deregulation of Mitochondrial Membrane Potential by Mitochondrial Insertion of Granzyme B and Direct Hax-1 Cleavage

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

Assessing the role of residue E73 and lipid headgroup charge in VDAC1 voltage gating

Queralt-Martín, M., Bergdoll, L. A., Jacobs, D., Bezrukov, S. M., Abramson, J., & Rostovtseva, T. K. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.11.001 · Cited by 43 · see citing works

Reflections on VDAC as a voltage-gated channel and a mitochondrial regulator

Mannella, C. A., & Kinnally, K. W. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9143-0 · Cited by 41 · see citing works

Different apoptotic effects of wogonin via induction of H2O2 generation and Ca2+ overload in malignant hepatoma and normal hepatic cells

Wei, L., Lu, N., Dai, Q., Rong, J., Chen, Y., Li, Z., You, Q., & Guo, Q. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22898 · Cited by 39 · see citing works

Mitoxosome: a mitochondrial platform for cross‐talk between cellular stress and antiviral signaling

Tal, M. C., & Iwasaki, A. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01038.x · Cited by 38 · see citing works

Palladacycles catalyse the oxidation of critical thiols of the mitochondrial membrane proteins and lead to mitochondrial permeabilization and cytochrome c release associated with apoptosis

Santana, D. P., de Faria, P. A., Paredes‐Gamero, E. J., Caires, A. C. F., Nantes, I. L., & Rodrigues, T. (2008) · Biochemical Journal · doi:10.1042/bj20080972 · Cited by 39 · see citing works

Neuroprotective and neurorestorative potential of propargylamine derivatives in ageing: focus on mitochondrial targets

Bar‐Am, O., Amit, T., Youdim, M. B. H., & Weinreb, O. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1395-3 · Cited by 36 · see citing works

Phytochemicals and mitochondria: Therapeutic allies against gastric cancer

Zhao, M., Yang, Y., Nian, Q., Shen, C., Xiao, X., Liao, W., Zheng, Q., Zhang, G., Chen, N., Gong, D., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154608 · Cited by 36 · see citing works

Muscle FBPase binds to cardiomyocyte mitochondria under glycogen synthase kinase‐3 inhibition or elevation of cellular Ca2+ level

Gizak, A., Piróg, M., & Rakus, D. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.032 · Cited by 33 · see citing works

Meningococcal Porin PorB Prevents Cellular Apoptosis in a Toll-Like Receptor 2- and NF-κB-Independent Manner

Massari, P., Gunawardana, J., Liu, X., & Wetzler, L. M. (2009) · Infection and Immunity · doi:10.1128/iai.00156-09 · Cited by 33 · see citing works

Apoptosis: it's BAK to VDAC

Shore, G. C. (2009) · EMBO Reports · doi:10.1038/embor.2009.249 · Cited by 27 · see citing works

Novel insights into the mitochondrial permeability transition

Bonora, M., Pedro, J. M. B., Kroemer, G., Galluzzi, L., & Pinton, P. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949082 · Cited by 22 · see citing works

Characterization of Oyster Voltage-Dependent Anion Channel 2 (VDAC2) Suggests Its Involvement in Apoptosis and Host Defense

Li, Y., Zhang, L., Qu, T., Li, L., & Zhang, G. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146049 · Cited by 19 · see citing works

In vitro mitochondrial effects of PK 11195, a synthetic translocator protein 18 kDa (TSPO) ligand, in human osteoblast-like cells

Rosenberg, N., Rosenberg, O., Weizman, A., Leschiner, S., Sakoury, Y., Fares, F., Soudry, M., Weisinger, G., Veenman, L., & Gavish, M. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9388-x · Cited by 18 · see citing works

Cyclophilin D: Guardian or Executioner for Tumor Cells?

Zhang, L., Liu, Y., Zhou, R. L., He, B., Wang, W., & Zhang, B. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.939588 · Cited by 16 · see citing works

The mitochondrial outer membrane protein import machinery: a new player in apoptosis?

Petit, E. (2009) · Frontiers in bioscience · doi:10.2741/3471 · Cited by 16 · see citing works

Evaluation of Anticancer and Immunomodulatory Effects of Microwave-Extracted Polysaccharide from Ruditapes philippinarum

Liu, M., Li, F., Feng, S., Guo, J., Yu, J., Zou, S., Gao, X., & Wei, Y. (2024) · Foods · doi:10.3390/foods13223552 · Cited by 12 · see citing works

Comprehensive analysis of regulated cell death pathways: intrinsic disorder, protein–protein interactions, and cross-pathway communication

Sorokin, O., Hause, F., Wedler, A., Alakhras, T., Bauchspiess, T., Dietrich, A., Günther, W. F., Guha, C., Obika, K. B., Kraft, J., et al. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02161-6 · Cited by 11 · see citing works

Targeted Modulation of Mitochondrial Oxidative Stress Ameliorates 5‐Fluorouracil‐Induced Renal Injury in BALB/c Mice

Tambe, P. K., Shetty, M. P., Rana, K., & Bharati, S. (2025) · Oxidative Medicine and Cellular Longevity · doi:10.1155/omcl/8892026 · Cited by 8 · see citing works

Multiple entanglements of different cell death pathways, in which caspase-8 and BID interact with cardiolipin*, have been identified

PETIT, P. X. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1667611 · Cited by 7 · see citing works

Determining Signalling Nodes for Apoptosis by a Genetic High-Throughput Screen

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Pathophysiology of Cancer Cell Death

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Mitochondrial Alteration: A Major Player in Carcinogenesis

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Cell Injury and Necrosis

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The Molecular Mechanism of Human Voltage-Dependent Anion Channel 1 Blockade by the Metallofullerenol Gd@C82(OH)22: An In Silico Study

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Pathophysiology of Cancer Cell Death

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VI-16, a newly synthesized flavonoid, induces apoptosis through the mitochondrial pathway in human hepatoma cells

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Putative Remedial Effect of Zinc Oxide Nanoparticles on the Apoptotic Response in Nile Tilapia Exposed to Potential Micro Plastics in Sewage Effluent

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CYPD limits HR+ mammary carcinogenesis in mice

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Mitochondria in Cell Death Regulation

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Chaîne respiratoire et pore de transition de perméabilité mitochondriale dans la cardioprotection

Li, B. (2009) · doi:10.70675/53a81cafz7ff6z4866z9cbfzc2644e901846 · Cited by 1 · see citing works

Untersuchung sub-mitochondrialer Proteinverteilungen in unbehandelten und apoptotischen humanen Zellen mittels STED-Mikroskopie

Neumann, D. (2010) · doi:10.53846/goediss-383

Cell Death Mechanisms, Associated Toxicity and Therapeutic Applications

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Intrinsic Apoptotic Pathway: Effects of Calcium on Murine Cytochrome C Release in Brain and Liver Mitochondria

Edwards, D. M. (2013) · Digital Commons (Liberty University)

The role of VDAC in cell death: Friend or foe?

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The Mitochondrial Voltage-dependent Anion Channel (VDAC) as a Therapeutic Target for Initiating Cell Death

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Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

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VDAC, a multi-functional mitochondrial protein regulating cell life and death

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The Voltage-Dependent Anion Channel (VDAC): Function in Intracellular Signalling, Cell Life and Cell Death

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