Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c

Cell Death: The Significance of Apoptosis

Wyllie, A. H., Kerr, J. F. R., & Currie, A. R. (1980) · International review of cytology · doi:10.1016/s0074-7696(08)62312-8 · Cited by 7,151

Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation

Wyllie, A. H. (1980) · Nature · doi:10.1038/284555a0 · Cited by 4,499

Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A., et al. (1995) · Nature · doi:10.1038/376037a0 · Cited by 3,980

Bcl-2 functions in an antioxidant pathway to prevent apoptosis

Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,402

A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes

Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme

Ji, Y. (1993) · Cell · doi:10.1016/0092-8674(93)90485-9 · Cited by 2,497

Mechanisms and Genes of Cellular Suicide

Steller, H. (1995) · Science · doi:10.1126/science.7878463 · Cited by 2,469

Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

Tewari, M., Quan, L. T., O’Rourke, K. M., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S., & Dixit, V. M. (1995) · Cell · doi:10.1016/0092-8674(95)90541-3 · Cited by 2,367

Bcl-2 and the regulation of programmed cell death

Reed, J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.1.1 · Cited by 2,287

Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis.

Kaufmann, S. H., Desnoyers, S., Ottaviano, Y. L., Davidson, N. E., & Poirier, G. G. (1993) · PubMed · Cited by 1,889

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289

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

The Inflammasome

Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066

Cell Death

Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587

Mitochondrial formation of reactive oxygen species

Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084

Molecular characterization of mitochondrial apoptosis-inducing factor

Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626

Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition

Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513

Mitochondrial diseases in man and mouse

Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060

Mitochondrial TCA cycle metabolites control physiology and disease

Martínez-Reyes, I., & Chandel, N. S. (2020) · Nature Communications · doi:10.1038/s41467-019-13668-3 · Cited by 2,813

Physiological Roles of Mitochondrial Reactive Oxygen Species

Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632

Calcium, ATP, and ROS: a mitochondrial love-hate triangle

Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575

The mitochondrial permeability transition pore and its role in cell death

CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125

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

The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis

Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755

High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria

Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727

Comparative Genomics of the Eukaryotes

Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698

Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9

Kuida, K., Haydar, T. F., Kuan, C.-Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S.-S., Rakic, P., & Flavell, R. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81476-2 · Cited by 1,643

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550

The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy

Lemasters, J. J., Nieminen, A.-L., Qian, T., Trost, L. C., Elmore, S. P., Nishimura, Y., Crowe, R. A., Cascio, W. E., Bradham, C. A., Brenner, D. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00112-1 · Cited by 1,387

Mitochondrial dynamics and apoptosis

Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270

Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD‐specific caspase activation and independently of mitochondrial transmembrane depolarization

Bossy‐Wetzel, E., Newmeyer, D. D., & Green, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.1.37 · Cited by 1,225

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

Caspases in apoptosis and beyond

Li, J., & Yuan, J. (2008) · Oncogene · doi:10.1038/onc.2008.297 · Cited by 1,090

Caspase Cleaved BID Targets Mitochondria and Is Required for Cytochrome c Release, while BCL-XL Prevents This Release but Not Tumor Necrosis Factor-R1/Fas Death

Gross, A., Yin, X.-M., Wang, K., Wei, M. C., Jockel, J., Milliman, C., Erdjument-Bromage, H., Tempst, P., & Korsmeyer, S. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.1156 · Cited by 1,045

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

T cell apoptosis by tryptophan catabolism

Fallarino, F., Grohmann, U., Vacca, C., Bianchi, R., Orabona, C., Spreca, A., Fioretti, M. C., & Puccetti, P. (2002) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401073 · Cited by 1,022

Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis

Yin, X.-M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., Roth, K. A., & Korsmeyer, S. J. (1999) · Nature · doi:10.1038/23730 · Cited by 1,004

Uncoupling: new approaches to an old problem of bioenergetics

Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893

Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864

Cell-permeable Peptide Antioxidants Targeted to Inner Mitochondrial Membrane inhibit Mitochondrial Swelling, Oxidative Cell Death, and Reperfusion Injury

Zhao, K., Zhao, G.-M., Wu, D., Soong, Y., Birk, A. V., Schiller, P. W., & Szeto, H. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402999200 · Cited by 782

Free Radical Pathways in CNS Injury

LEWÉN, A., MATZ, P., & CHAN, P. H. (2000) · Journal of Neurotrauma · doi:10.1089/neu.2000.17.871 · Cited by 759

Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies

Delbridge, A. R. D., Grabow, S., Strasser, A., & Vaux, D. L. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.17 · Cited by 752

A “mitochondrial cascade hypothesis” for sporadic Alzheimer’s disease

Swerdlow, R. H., & Khan, S. M. (2004) · Medical Hypotheses · doi:10.1016/j.mehy.2003.12.045 · Cited by 758

Nitric oxide and mitochondrial respiration

Brown, G. C. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00025-0 · Cited by 702

Role of mitochondria in oxidative stress and ageing

Lenaz, G. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00120-0 · Cited by 650

The mitochondrial pathways of apoptosis

Estaquier, J., Vallette, F., Vayssiere, J.-L., & Mignotte, B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_7 · Cited by 637

The mitochondrial permeability transition from in vitro artifact to disease target

Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627

Initiation and execution mechanisms of necroptosis: an overview

Grootjans, S., Vanden Berghe, T., & Vandenabeele, P. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.65 · Cited by 566

Mitochondria as signaling organelles

Chandel, N. S. (2014) · BMC Biology · doi:10.1186/1741-7007-12-34 · Cited by 576

Oxidative stress in the brain: Novel cellular targets that govern survival during neurodegenerative disease

Chong, Z. Z., Li, F., & Maiese, K. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.02.004 · Cited by 536

DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: fail-safe protection against carcinogenesis

Bernstein, C. (2002) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(02)00009-1 · Cited by 527

New insights into the role of mitochondria in aging: mitochondrial dynamics and more

Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522

Cytochrome c Deficiency Causes Embryonic Lethality and Attenuates Stress-Induced Apoptosis

Li, K., Li, Y., Shelton, J. M., Richardson, J. A., Spencer, E., Chen, Z. J., Wang, X., & Williams, R. S. (2000) · Cell · doi:10.1016/s0092-8674(00)80849-1 · Cited by 509

On the role of Hsp27 in regulating apoptosis

Concannon, C. G., Gorman, A. M., & Samali, A. (2003) · Apoptosis · doi:10.1023/a:1021601103096 · Cited by 513

The Mitochondrial Permeability Transition, Release of Cytochrome c and Cell Death

Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P., & Di Lisa, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010604200 · Cited by 472

Dying cells actively regulate adaptive immune responses

Yatim, N., Cullen, S., & Albert, M. L. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.9 · Cited by 442

The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice

Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438

Translocation of SAPK/JNK to Mitochondria and Interaction with Bcl-xL in Response to DNA Damage

Kharbanda, S., Saxena, S., Yoshida, K., Pandey, P., Kaneki, M., Wang, Q., Cheng, K., Chen, Y.-N., Campbell, A., Sudha, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.322 · Cited by 429

Mitochondrial endonuclease G is important for apoptosis in C. elegans

Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., & Xue, D. (2001) · Nature · doi:10.1038/35083608 · Cited by 427

In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death

AZOULAY-ZOHAR, H., ISRAELSON, A., ABU-HAMAD, S., & SHOSHAN-BARMATZ, V. (2004) · Biochemical Journal · doi:10.1042/bj20031465 · Cited by 408

How biology handles nitrite

Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401

Mechanisms of AIF-Mediated Apoptotic DNA Degradation in Caenorhabditis elegans

Wang, X., Yang, C., Chai, J., Shi, Y., & Xue, D. (2002) · Science · doi:10.1126/science.1076194 · Cited by 393

The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis

Wong, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.3.425 · Cited by 374

Bcl-x Promotes the Open Configuration of the Voltage-dependent Anion Channel and Metabolite Passage through the Outer Mitochondrial Membrane

Vander Heiden, M. G., Li, X. X., Gottleib, E., Hill, R. B., Thompson, C. B., & Colombini, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101590200 · Cited by 372

The Peroxisome-Mitochondria Connection: How and Why?

Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351

Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach

Sultana, R., Poon, H. F., Cai, J., Pierce, W. M., Merchant, M., Klein, J. B., Markesbery, W. R., & Butterfield, D. A. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.10.004 · Cited by 364

Mitophagy: An Emerging Role in Aging and Age-Associated Diseases

Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359

Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions

Fernandez, P. M., Tabbara, S. O., Jacobs, L. K., Manning, F. C. R., Tsangaris, T. N., Schwartz, A. M., Kennedy, K. A., & Patierno, S. R. (2000) · Breast Cancer Research and Treatment · doi:10.1023/a:1006332011207 · Cited by 338

Mitochondria—Judges and Executioners of Cell Death Sentences

Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326

Concentration-dependent Effects of Nitric Oxide on Mitochondrial Permeability Transition and Cytochrome cRelease

Brookes, P. S., Salinas, E. P., Darley-Usmar, K., Eiserich, J. P., Freeman, B. A., Darley-Usmar, V. M., & Anderson, P. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001077200 · Cited by 321

Cell-permeable, mitochondrial-targeted, peptide antioxidants

Szeto, H. H. (2006) · The AAPS Journal · doi:10.1007/bf02854898 · Cited by 316

Phospholipid-Cytochrome c Interaction

Tuominen, E. K. J., Wallace, C. J. A., & Kinnunen, P. K. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200056200 · Cited by 309

Mitochondria, oxygen free radicals, and apoptosis

Raha, S., & Robinson, B. H. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1398 · Cited by 306

Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species

Brookes, P. S., Levonen, A.-L., Shiva, S., Sarti, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00901-2 · Cited by 298

Bax assembles into large ring‐like structures remodeling the mitochondrial outer membrane in apoptosis

Große, L., Wurm, C. A., Brüser, C., Neumann, D., Jans, D. C., & Jakobs, S. (2016) · The EMBO Journal · doi:10.15252/embj.201592789 · Cited by 281

Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis

Costantini, P., Belzacq, A.-S., Vieira, H. L., Larochette, N., de Pablo, M. A., Zamzami, N., Susin, S. A., Brenner, C., & Kroemer, G. (2000) · Oncogene · doi:10.1038/sj.onc.1203299 · Cited by 284

Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines

Zhao, K., Luo, G., Giannelli, S., & Szeto, H. H. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.08.022 · Cited by 251

The adenine nucleotide translocator: a target of nitric oxide, peroxynitrite, and 4-hydroxynonenal

Vieira, H. L., Belzacq, A.-S., Haouzi, D., Bernassola, F., Cohen, I., Jacotot, E., Ferri, K. F., El Hamel, C., Bartle, L. M., Melino, G., et al. (2001) · Oncogene · doi:10.1038/sj.onc.1204575 · Cited by 244

Apoptosis of Retinal Ganglion Cells in Glaucoma

Nickells, R. W. (1999) · Survey of Ophthalmology · doi:10.1016/s0039-6257(99)00029-6 · Cited by 232

Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination

Zirngibl, M., Assinck, P., Sizov, A., Caprariello, A. V., & Plemel, J. R. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00538-8 · Cited by 233

Low Reserve of Cytochrome c Oxidase Capacity in Vivo in the Respiratory Chain of a Variety of Human Cell Types

Villani, G., Greco, M., Papa, S., & Attardi, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31829 · Cited by 225

Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis

Jiang, X., Jiang, H., Shen, Z., & Wang, X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417253111 · Cited by 220

Parvalbumin interneuron vulnerability and brain disorders

Ruden, J. B., Dugan, L. L., & Konradi, C. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-0778-9 · Cited by 194

Energy Metabolism during Apoptosis

Garland, J. M., & Halestrap, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4680 · Cited by 207

Mitochondrial dynamics maintain muscle stem cell regenerative competence throughout adult life by regulating metabolism and mitophagy

Hong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213

Cathepsin B: A sellsword of cancer progression

Mijanović, O., Branković, A., Panin, A. N., Savchuk, S., Timashev, P., Ulasov, I., & Lesniak, M. S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.035 · Cited by 205

Eukaryotic Translation Initiation Factor 4G Is Targeted for Proteolytic Cleavage by Caspase 3 during Inhibition of Translation in Apoptotic Cells

Marissen, W. E., & Lloyd, R. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7565 · Cited by 198

Spatial Distribution of Bax and Bcl-2 in Osteocytes After Bone Fatigue: Complementary Roles in Bone Remodeling Regulation?

Verborgt, O., Tatton, N. A., Majeska, R. J., & Schaffler, M. B. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.5.907 · Cited by 192

Bid acts on the permeability transition pore complex to induce apoptosis

Zamzami, N., Hamel, C. E., Maisse, C., Brenner, C., Muñoz-Pinedo, C., Belzacq, A.-S., Costantini, P., Vieira, H., Loeffler, M., Molle, G., et al. (2000) · Oncogene · doi:10.1038/sj.onc.1204030 · Cited by 178

Oxygen sensing in yeast: Evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes

Kwast, K. E., Burke, P. V., Staahl, B. T., & Poyton, R. O. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5446 · Cited by 175

BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore

Walensky, L. D., & Gavathiotis, E. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.08.009 · Cited by 173

Electron microscopic tomography of rat‐liver mitochondria and their interactions with the endoplasmic reticulum

Mannella, C. A., Buttle, K., Rath, B. K., & Marko, M. (1998) · BioFactors · doi:10.1002/biof.5520080309 · Cited by 167

Membrane-linked systems preventing superoxide formation

Skulachev, V. P. (1997) · Bioscience Reports · doi:10.1023/a:1027344914565 · Cited by 162

Mitochondrial contact sites: their role in energy metabolism and apoptosis

Brdiczka, D. G., Zorov, D. B., & Sheu, S.-S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.09.007 · Cited by 150

Interaction of peroxidized cardiolipin with rat‐heart mitochondrial membranes: Induction of permeability transition and cytochrome c release

Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137

A break in mitochondrial endosymbiosis as a basis for inflammatory diseases

Murphy, M. P., & O’Neill, L. A. J. (2024) · Nature · doi:10.1038/s41586-023-06866-z · Cited by 138

Hypothesis: the mitochondrial NO(*) signaling pathway, and the transduction of nitrosative to oxidative cell signals: an alternative function for cytochrome c oxidase

Brookes, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00805-x · Cited by 137

Akt Phosphorylates MstI and Prevents Its Proteolytic Activation, Blocking FOXO3 Phosphorylation and Nuclear Translocation

Jang, S.-W., Yang, S.-J., Srinivasan, S., & Ye, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704542200 · Cited by 133

Interaction of Peroxynitrite with Mitochondrial Cytochrome Oxidase

Sharpe, M. A., & Cooper, C. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.30961 · Cited by 133

Ethanol-Induced Apoptosis in Mouse Liver

Zhou, Z., Sun, X., & Kang, Y. J. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)61699-9 · Cited by 129

Effect of Cytochrome c on the Generation and Elimination of O2⨪ and H2O2 in Mitochondria

Zhao, Y., Wang, Z.-B., & Xu, J.-X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209681200 · Cited by 129

The Three Families of Respiratory NADH Dehydrogenases

Kerscher, S., Dröse, S., Zickermann, V., & Brandt, U. (2007) · Results and Problems in Cell Differentiation · doi:10.1007/400_2007_028 · Cited by 127

Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity

Chen, Y.-R., Deterding, L. J., Sturgeon, B. E., Tomer, K. B., & Mason, R. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200709200 · Cited by 110

Dysregulated autophagy contributes to caspase-dependent neuronal apoptosis

Chung, Y., Lee, J., Jung, S., Lee, Y., Cho, J. W., & Oh, Y. J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-1229-y · Cited by 99

Extracellular cytochrome c, a mitochondrial apoptosis-related protein, induces arthritis

Pullerits, R., Bokarewa, M., Jonsson, I.-M., Verdrengh, M., & Tarkowski, A. (2005) · Rheumatology · doi:10.1093/rheumatology/keh406 · Cited by 86

Mitochondria-cytosol-nucleus crosstalk: learning from Saccharomyces cerevisiae

Guaragnella, N., Coyne, L. P., Chen, X. J., & Giannattasio, S. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy088 · Cited by 72

Severe mitochondrial damage associated with low-dose radiation sensitivity in ATM- and NBS1-deficient cells

Shimura, T., Kobayashi, J., Komatsu, K., & Kunugita, N. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1156276 · Cited by 55

Cell Stress-Associated Caspase Activation: Intrinsically Complex?

Creagh, E. M., & Martin, S. J. (2003) · Science s STKE · doi:10.1126/stke.2003.175.pe11 · Cited by 15

Mitochondrial regulation of insect cell apoptosis: Evidence for permeability transition pore-independent cytochrome-c release in the Lepidopteran Sf9 cells

Kumarswamy, R., Seth, R. K., Dwarakanath, B. S. R., & Chandna, S. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.12.009 · Cited by 84

Targeting the Apoptosome for Cancer Therapy

Ledgerwood, E. C., & Morison, I. M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1172 · Cited by 102

Gold opens mitochondrial pathways to apoptosis

McKeage, M. J. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704822 · Cited by 25

Bax membrane insertion during Fas(CD95)-induced apoptosis precedes cytochrome c release and is inhibited by Bcl-2

Murphy, K. M., Streips, U. N., & Lock, R. B. (1999) · Oncogene · doi:10.1038/sj.onc.1203001 · Cited by 89