Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3

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

Death Receptors: Signaling and Modulation

Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866

Cell Death

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

The Bcl2 family: regulators of the cellular life-or-death switch

Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032

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

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219

Two CD95 (APO‐1/Fas) signaling pathways

Scaffidi, C., Fulda, S., Srinivasan, A., Friesen, C., Li, F., Tomaselli, K. J., Debatin, K., Krammer, P. H., & Peter, M. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1675 · Cited by 3,000

Regulation of Cell Death Protease Caspase-9 by Phosphorylation

Cardone, M. H., Roy, N., Stennicke, H. R., Salvesen, G. S., Franke, T. F., Stanbridge, E., Frisch, S., & Reed, J. C. (1998) · Science · doi:10.1126/science.282.5392.1318 · Cited by 2,481

The mitochondrial permeability transition pore and its role in cell death

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

Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012

Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421

Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins

Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., & Vaux, D. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00009-x · Cited by 2,372

Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy

Fulda, S., & Debatin, K.-M. (2006) · Oncogene · doi:10.1038/sj.onc.1209608 · Cited by 2,312

Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112

IAP proteins: blocking the road to death's door

Salvesen, G. S., & Duckett, C. S. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm830 · Cited by 1,756

Requirement of JNK for Stress- Induced Activation of the Cytochrome c-Mediated Death Pathway

Tournier, C., Hess, P., Yang, D. D., Xu, J., Turner, T. K., Nimnual, A., Bar-Sagi, D., Jones, S. N., Flavell, R. A., & Davis, R. J. (2000) · Science · doi:10.1126/science.288.5467.870 · Cited by 1,728

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

A matter of life and death

Green, D. R., & Evan, G. I. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00024-7 · Cited by 1,254

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

Anoikis molecular pathways and its role in cancer progression

Paoli, P., Giannoni, E., & Chiarugi, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.026 · Cited by 1,160

The apoptosome: Signalling platform of cell death

Riedl, S. J., & Salvesen, G. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2153 · Cited by 1,097

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

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

Caspases and their substrates

Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816

Brain ischemia and reperfusion: molecular mechanisms of neuronal injury

White, B. C., Sullivan, J. M., DeGracia, D. J., O’Neil, B. J., Neumar, R. W., Grossman, L. I., Rafols, J. A., & Krause, G. S. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00386-5 · Cited by 796

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

Nod1, an Apaf-1-like Activator of Caspase-9 and Nuclear Factor-κB

Inohara, N., Koseki, T., del Peso, L., Hu, Y., Yee, C., Chen, S., Carrio, R., Merino, J., Liu, D., Ni, J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14560 · Cited by 742

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

Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer

Catz, S. D., & Johnson, J. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204926 · Cited by 538

From pyroptosis, apoptosis and necroptosis to PANoptosis: A mechanistic compendium of programmed cell death pathways

Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545

VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release

Madesh, M., & Hajnóczky, G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200105057 · Cited by 538

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

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

Caspase-9 Can Be Activated without Proteolytic Processing

Stennicke, H. R., Deveraux, Q. L., Humke, E. W., Reed, J. C., Dixit, V. M., & Salvesen, G. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8359 · Cited by 497

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

Recruitment, activation and retention of caspases‐9 and ‐3 by Apaf‐1 apoptosome and associated XIAP complexes

Bratton, S. B., Walker, G., Srinivasula, S. M., Sun, X., Butterworth, M., Alnemri, E. S., & Cohen, G. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.998 · Cited by 406

NLRs at the intersection of cell death and immunity

Ting, J. P.-Y., Willingham, S. B., & Bergstralh, D. T. (2008) · Nature Reviews Immunology · doi:10.1038/nri2296 · Cited by 371

Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling

Gorman, A. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00402.x · Cited by 362

Molecular aspects of glutamate dysregulation: implications for schizophrenia and its treatment

Konradi, C., & Heckers, S. (2003) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00328-5 · Cited by 336

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

Amyloid‐Beta Interaction with Mitochondria

Pagani, L., & Eckert, A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/925050 · Cited by 309

Neuronal death/survival signaling pathways in cerebral ischemia

Sugawara, T., Fujimura, M., Noshita, N., Kim, G. W., Saito, A., Hayashi, T., Narasimhan, P., Maier, C. M., & Chan, P. H. (2004) · NeuroRX · doi:10.1602/neurorx.1.1.17 · Cited by 270

Supplementation of Endothelial Cells with Mitochondria-targeted Antioxidants Inhibit Peroxide-induced Mitochondrial Iron Uptake, Oxidative Damage, and Apoptosis

Dhanasekaran, A., Kotamraju, S., Kalivendi, S. V., Matsunaga, T., Shang, T., Keszler, A., Joseph, J., & Kalyanaraman, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404003200 · Cited by 241

Autophagic Cell Death and Its Execution by Lysosomal Cathepsins.

UCHIYAMA, Y. (2001) · Archives of Histology and Cytology · doi:10.1679/aohc.64.233 · Cited by 243

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

The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation

Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229

Human complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect

Robinson, B. H. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00033-4 · Cited by 223

The mitochondrial permeability transition

Bernardi, P., Colonna, R., Costantini, P., Eriksson, O., Fontaine, E., Ichas, F., Massari, S., Nicolli, A., Petronilli, V., & Scorrano, L. (1998) · BioFactors · doi:10.1002/biof.5520080315 · Cited by 183

A Bax-Induced Pro-Oxidant State Is Critical for Cytochrome c Release during Programmed Neuronal Death

Kirkland, R. A., Windelborn, J. A., Kasprzak, J. M., & Franklin, J. L. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06480.2002 · Cited by 165

Defining the Origins of the NOD-Like Receptor System at the Base of Animal Evolution

Lange, C., Hemmrich, G., Klostermeier, U. C., Lopez-Quintero, J. A., Miller, D. J., Rahn, T., Weiss, Y., Bosch, T. C. G., & Rosenstiel, P. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msq349 · Cited by 150

WISP-1 attenuates p53-mediated apoptosis in response to DNA damage through activation of the Akt kinase

Su, F., Overholtzer, M., Besser, D., & Levine, A. J. (2002) · Genes & Development · doi:10.1101/gad.942902 · Cited by 153

Apoptosis regulators and responses in human melanocytic and keratinocytic cells

Bowen, A. R., Hanks, A. N., Allen, S. M., Alexander, A., Diedrich, M. J., & Grossman, D. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12010.x · Cited by 149

Differential regulation of apoptotic cell death in senescent human cells.

Hampel, B., Malisan, F., Niederegger, H., Testi, R., & Jansen-Dürr, P. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.05.010 · Cited by 133

Alternative Germ Cell Death Pathway in Drosophila Involves HtrA2/Omi, Lysosomes, and a Caspase-9 Counterpart

Yacobi-Sharon, K., Namdar, Y., & Arama, E. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.02.002 · Cited by 119

Caspase-9 is activated in a cytochrome c-independent manner early during TNFα-induced apoptosis in murine cells

McDonnell, M. A., Wang, D., Khan, S. M., Vander Heiden, M. G., & Kelekar, A. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401271 · Cited by 109

Targeting MCL-1 protein to treat cancer: opportunities and challenges

Tantawy, S. I., Timofeeva, N., Sarkar, A., & Gandhi, V. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1226289 · Cited by 90

Untitled work

(2002) · PubMed · Cited by 89

Dynamin-related protein 1 mediates high glucose induced pancreatic beta cell apoptosis

Men, X., Wang, H., Li, M., Cai, H., Xu, S., Zhang, W., Xu, Y., Ye, L., Yang, W., Wollheim, C. B., et al. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.031 · Cited by 83

Small molecule modulators of protein-protein interactions: selected case studies

Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79

Frequent LOH at Chromosome 12q22‐23 and Apaf‐1 Inactivation in Glioblastoma

Watanabe, T., Hirota, Y., Arakawa, Y., Fujisawa, H., Tachibana, O., Hasegawa, M., Yamashita, J., & Hayashi, Y. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00474.x · Cited by 55

Ceramide Induces Release of Pro-Apoptotic Proteins from Mitochondria by Either a Ca2+-Dependent or a Ca2+-Independent Mechanism

Di Paola, M., Zaccagnino, P., Montedoro, G., Cocco, T., & Lorusso, M. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000023619.97392.0c · Cited by 52

Role of reactive oxygen species-elicited apoptosis in the pathophysiology of mitochondrial and neurodegenerative diseases associated with mitochondrial DNA mutations

Liu, C.-Y., Lee, C.-F., & Wei, Y.-H. (2009) · Journal of the Formosan Medical Association · doi:10.1016/s0929-6646(09)60380-6 · Cited by 52

Autophagic and apoptotic features during programmed cell death in the fat body of the tobacco hornworm (Manduca sexta)

Müller, F., Ádori, C., & Sass, M. (2004) · European Journal of Cell Biology · doi:10.1078/0171-9335-00359 · Cited by 49

Apoptotic cell death in neurons and glial cells: implications for Alzheimer's disease

Yoshihisa, K., Takashi, T., & Shun, S. (1999) · Japanese Journal of Pharmacology · doi:10.1254/jjp.79.1 · Cited by 47

Cytochrome c, released from cerebellar granule cells undergoing apoptosis or excytotoxic death, can generate protonmotive force and drive ATP synthesis in isolated mitochondria

Atlante, A., De Bari, L., Bobba, A., Marra, E., Calissano, P., & Passarella, S. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01863.x · Cited by 45

Bax mRNA therapy using cationic liposomes for human malignant melanoma

Okumura, K., Nakase, M., Inui, M., Nakamura, S., Watanabe, Y., & Tagawa, T. (2008) · The Journal of Gene Medicine · doi:10.1002/jgm.1214 · Cited by 31