IAP proteins: blocking the road to death's door

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673 · see citing works

Apoptosis in the Pathogenesis and Treatment of Disease

Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524 · see citing works

NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses

Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182 · see citing works

Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis

Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445 · see citing works

Identification and characterization of a spinal muscular atrophy-determining gene

Lefebvre, S., Bürglen, L., Reboullet, S., Clermont, O., Burlet, P., Viollet, L., Bénichou, B., Cruaud, C., Millasseau, P., Zeviani, M., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90460-3 · Cited by 3,995 · see citing works

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 · see citing works

A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma

Ambrosini, G., Adida, C., & Altieri, D. C. (1997) · Nature Medicine · doi:10.1038/nm0897-917 · Cited by 3,167 · see citing works

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

Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80501-2 · Cited by 3,145 · see citing works

NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation.

Wang, C.-Y., Mayo, M., Korneluk, R., Goeddel, D., & Baldwin, A. (1998) · Science · doi:10.1126/science.281.5383.1680 · Cited by 2,950 · see citing works

Programmed Cell Death in Animal Development

Jacobson, M. D., Weil, M., & RAFF, M. C. (1997) · Cell · doi:10.1016/s0092-8674(00)81873-5 · Cited by 2,685 · see citing works

Biochemical Pathways of Caspase Activation During Apoptosis

Budihardjo, I. I., Oliver, H., Lutter, M. L., Luo, X., & Wang, X. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.269 · Cited by 2,562 · see citing works

Inhibition of death receptor signals by cellular FLIP

Irmler, M., Thome, M., Hahne, M., Schneider, P., Hofmann, K., Steiner, V., Bodmer, J.-L., Schröter, M., Burns, K., Mattmann, C., et al. (1997) · Nature · doi:10.1038/40657 · Cited by 2,548 · see citing works

IAP family proteins---suppressors of apoptosisPreprint

Deveraux, Q. L., & Reed, J. C. (1999) · Genes & Development · doi:10.1101/gad.13.3.239 · Cited by 2,535 · see citing works

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 · see citing works

FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis

Chinnaiyan, A. M., O'Rourke, K., Tewari, M., & Dixit, V. M. (1995) · Cell · doi:10.1016/0092-8674(95)90071-3 · Cited by 2,431 · see citing works

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 · see citing works

Cytotoxicity‐dependent APO‐1 (Fas/CD95)‐associated proteins form a death‐inducing signaling complex (DISC) with the receptor.

Kischkel, F. C., Hellbardt, S., Behrmann, I., Germer, M., Pawlita, M., Krammer, P. H., & Peter, M. E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00245.x · Cited by 2,181 · see citing works

X-linked IAP is a direct inhibitor of cell-death proteases

Deveraux, Q. L., Takahashi, R., Salvesen, G. S., & Reed, J. C. (1997) · Nature · doi:10.1038/40901 · Cited by 1,956 · see citing works

Control of apoptosis and mitotic spindle checkpoint by survivin

Li, F., Ambrosini, G., Chu, E. Y., Plescia, J., Tognin, S., Marchisio, P. C., & Altieri, D. C. (1998) · Nature · doi:10.1038/25141 · Cited by 1,868 · see citing works

Mechanisms of Caspase Activation and Inhibition during Apoptosis

Shi, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00482-3 · Cited by 1,824 · see citing works

BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis

Cheng, E. H. Y., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., & Korsmeyer, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00320-3 · Cited by 1,708 · see citing works

Caspase structure, proteolytic substrates, and function during apoptotic cell death

Nicholson, D. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400598 · Cited by 1,540 · see citing works

Themes and variations on ubiquitylation

Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,472 · see citing works

IAPs block apoptotic events induced by caspase‐8 and cytochrome c by direct inhibition of distinct caspases

Deveraux, Q. L., Roy, N., Stennicke, H. R., Arsdale, T. V., Zhou, Q., Srinivasula, S. M., Alnemri, E. S., Salvesen, G. S., & Reed, J. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.8.2215 · Cited by 1,390 · see citing works

Identification of a Member of the MAPKKK Family as a Potential Mediator of TGF-β Signal Transduction

Yamaguchi, T., Shirakabe, K., Shibuyà, H., Irie, K., Oishi, I., Ueno, N., Taniguchi, T., Nishida, E., & Matsumoto, K. (1995) · Science · doi:10.1126/science.270.5244.2008 · Cited by 1,344 · see citing works

The c‐IAP‐1 and c‐IAP‐2 proteins are direct inhibitors of specific caspases

Roy, N., Deveraux, Q. L., Takahashi, R., Salvesen, G. S., & Reed, J. C. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.6914 · Cited by 1,302 · see citing works

RING Finger Proteins

Joazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249 · see citing works

Protein regulation by monoubiquitin

Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,213 · see citing works

FLICE is activated by association with the CD95 death‐inducing signaling complex (DISC)

Medema, J. P., Scaffidi, C., Kischkel, F. C., Shevchenko, A., Mann, M., Krammer, P. H., & Peter, M. E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.10.2794 · Cited by 1,189 · see citing works

A Serine Protease, HtrA2, Is Released from the Mitochondria and Interacts with XIAP, Inducing Cell Death

Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., & Takahashi, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00341-0 · Cited by 1,116 · see citing works

An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif

Crook, N. E., Clem, R. J., & Miller, L. K. (1993) · Journal of Virology · doi:10.1128/jvi.67.4.2168-2174.1993 · Cited by 1,058 · see citing works

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

Rothe, M., Pan, M.-G., Henzel, W. J., Ayres, T. M., & V. Goeddel, D. (1995) · Cell · doi:10.1016/0092-8674(95)90149-3 · Cited by 1,030 · see citing works

A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

Srinivasula, S. M., Hegde, R. P., Saleh, A., Datta, P., Shiozaki, E. N., Chai, J., Lee, R., Robbins, P. D., Fernandes‐Alnemri, T., Shi, Y., et al. (2001) · Nature · doi:10.1038/35065125 · Cited by 1,013 · see citing works

Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes

Listen, P., Roy, N., Tamai, K., Lefebvre, C. A., Baird, S. D., Cherton-Horvat, G., Farahani, R., McLean, M., lkeda, J.-E., MacKenzie, A., et al. (1996) · Nature · doi:10.1038/379349a0 · Cited by 1,005 · see citing works

Ubiquitin Protein Ligase Activity of IAPs and Their Degradation in Proteasomes in Response to Apoptotic Stimuli

Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M., & Ashwell, J. D. (2000) · Science · doi:10.1126/science.288.5467.874 · Cited by 981 · see citing works

The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy

Roy, N., Mahadevan, M. S., McLean, M., Shutter, G., Yaraghi, Z., Farahani, R. M., Baird, S. D., Besner-Johnston, A., Lefebvre, C. A., Kang, X., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90461-1 · Cited by 974 · see citing works

Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma

Uren (2000) · Molecular Cell · Cited by 971 · see citing works

Caspase activation: The induced-proximity model

Salvesen, G. S., & Dixit, V. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.10964 · Cited by 932 · see citing works

Three-Dimensional Structure of the Apoptosome

Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., & Akey, C. W. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00442-2 · Cited by 912 · see citing works

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 · see citing works

Structural basis of IAP recognition by Smac/DIABLO

Wu, G., Chai, J., Suber, T. L., Wu, J., Du, C., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35050012 · Cited by 863 · see citing works

Structural Basis for the Inhibition of Caspase-3 by XIAP

Riedl, S. J., Renatus, M., Schwarzenbacher, R., Zhou, Q., Sun, C. C., Fesik, S. W., Liddington, R., & Salvesen, G. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00274-4 · Cited by 793 · see citing works

The Rel/NF-κB Family Directly Activates Expression of the Apoptosis Inhibitor Bcl-x L

Chen, C., Edelstein, L. C., & Gélinas, C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2687-2695.2000 · Cited by 760 · see citing works

Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases

Deveraux, Q. L., Leo, E., Stennicke, H. R., Welsh, K., Salvesen, G. S., & Reed, J. C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5242 · Cited by 751 · see citing works

Identification of Omi/HtrA2 as a Mitochondrial Apoptotic Serine Protease That Disrupts Inhibitor of Apoptosis Protein-Caspase Interaction

Hegde, R. P., Srinivasula, S. M., Zhang, Z., Wassell, R. P., Mukattash, R., Cilenti, L., DuBois, G. C., Lazebnik, Y. A., Zervos, A. S., Fernandes‐Alnemri, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109721200 · Cited by 745 · see citing works

The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-κB that blocks TNFα-induced apoptosisPreprint

Zong, W.-X., Edelstein, L., Chen, C.-L., Bash, J., & Gélinas, C. (1999) · Genes & Development · doi:10.1101/gad.13.4.382 · Cited by 738 · see citing works

Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control

Chu, Z.-L., McKinsey, T. A., Liu, L., Gentry, J. J., Malim, M. H., & Ballard, D. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.19.10057 · Cited by 732 · see citing works

Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death

Hay, B. A., Wassarman, D. A., & Rubin, G. M. (1995) · Cell · doi:10.1016/0092-8674(95)90150-7 · Cited by 725 · see citing works

Inhibition of JNK activation through NF-κB target genes

Tang, G., Minemoto, Y., Dibling, B., Purcell, N. H., Li, Z., Karin, M., & Lin, A. (2001) · Nature · doi:10.1038/35104568 · Cited by 721 · see citing works

The Apoptosis Inhibitor Gene API2 and a Novel 18q Gene,MLT, Are Recurrently Rearranged in the t(11;18)(q21;q21) Associated With Mucosa-Associated Lymphoid Tissue Lymphomas

Dierlamm, J., Baens, M., Włodarska, I., Stefanova-Ouzounova, M., Hernández‐Rivas, J. M., HOSSFELD, D. K., Wolf‐Peeters, C. D., Hagemeijer, A., BERGHE, H. V. D., & Marynen, P. (1999) · Blood · doi:10.1182/blood.v93.11.3601 · Cited by 718 · see citing works

Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death

Suzuki, Y., Nakabayashi, Y., & Takahashi, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161506698 · Cited by 654 · see citing works

Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain

Liu, Z., Sun, C. C., Olejniczak, E. T., Meadows, R. P., Betz, S. F., Oost, T. K., Herrmann, J. E., Wu, J. C., & Fesik, S. W. (2000) · Nature · doi:10.1038/35050006 · Cited by 647 · see citing works

Identification of Paracaspases and Metacaspases Two Ancient Families of Caspase-like Proteins, One of which Plays a Key Role in MALT Lymphoma

Uren, A. G. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00094-0 · Cited by 638 · see citing works

A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors.

Duckett, C. S., Nava, V. E., Gedrich, R. W., Clem, R. J., Dongen, J. L. V., Gilfillan, M. C., Shiels, H., Hardwick, J. M., & Thompson, C. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00629.x · Cited by 633 · see citing works

Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias.

Tamm, I., Kornblau, S. M., Segall, H., Krajewski, S., Welsh, K., Kitada, S., Scudiero, D. A., Tudor, G., Qui, Y. H., Monks, A. P., et al. (2000) · PubMed · Cited by 610 · see citing works

Pleiotropic cell-division defects and apoptosis induced by interference with survivin function

Li, F., Ackermann, E. J., Bennett, C. F., Rothermel, A. L., Plescia, J., Tognin, S., Villa, A., Marchisio, P. C., & Altieri, D. C. (1999) · Nature Cell Biology · doi:10.1038/70242 · Cited by 600 · see citing works

TAB1: An Activator of the TAK1 MAPKKK in TGF-β Signal Transduction

Shibuyà, H., Yamaguchi, T., Shirakabe, K., Tonegawa, A., Gotoh, Y., Ueno, N., Irie, K., Nishida, E., & Matsumoto, K. (1996) · Science · doi:10.1126/science.272.5265.1179 · Cited by 587 · see citing works

Structural Basis of Caspase-7 Inhibition by XIAP

Chai, J., Shiozaki, E. N., Srinivasula, S. M., Wu, Q. Y., Dataa, P., Alnemri, E. S., & Shi, Y. (2001) · Cell · doi:10.1016/s0092-8674(01)00272-0 · Cited by 582 · see citing works

Caspase-9 and APAF-1 form an active holoenzymePreprint

Rodriguez, J., & Lazebnik, Y. A. (1999) · Genes & Development · doi:10.1101/gad.13.24.3179 · Cited by 573 · see citing works

HtrA2 Promotes Cell Death through Its Serine Protease Activity and Its Ability to Antagonize Inhibitor of Apoptosis Proteins

Verhagen, A. M., Silke, J., Ekert, P. G., Pakusch, M., Kaufmann, H., Connolly, L. M., Day, C. L., Tikoo, A., Burke, R., Wrobel, C. N., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109891200 · Cited by 558 · see citing works

The Serine Protease Omi/HtrA2 Regulates Apoptosis by Binding XIAP through a Reaper-like Motif

Martins, L. M., Iaccarino, I., Tenev, T., Gschmeissner, S., Totty, N. F., Lemoine, N. R., Savopoulos, J. W., Gray, C. W., Creasy, C. L., Dingwall, C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109784200 · Cited by 544 · see citing works

An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs

Birnbaum, M. J., Clem, R. J., & Miller, L. K. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2521-2528.1994 · Cited by 541 · see citing works

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 · see citing works

Nuclear Factor (NF)-κB–regulated X-chromosome–linked <i>iap</i> Gene Expression Protects Endothelial Cells from Tumor Necrosis Factor α–induced Apoptosis

Stehlik, C., de Martin, R., Kumabashiri, I., Schmid, J. A., Binder, B. R., & Lipp, J. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.1.211 · Cited by 532 · see citing works

Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype

Uren, A. G., Wong, L. H., Pakusch, M., Fowler, K. J., Burrows, F. J., Vaux, D. L., & Choo, K. H. A. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00769-7 · Cited by 527 · see citing works

Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors.

Uren, A. G., Pakusch, M., Hawkins, C. J., Puls, K. L., & Vaux, D. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4974 · Cited by 511 · see citing works

The Drosophila Caspase Inhibitor DIAP1 Is Essential for Cell Survival and Is Negatively Regulated by HID

Wang, S. L., Hawkins, C. J., Yoo, S. J., Müller, H. ‐. J., & Hay, B. A. (1999) · Cell · doi:10.1016/s0092-8674(00)81974-1 · Cited by 505 · see citing works

Tumor-cell resistance to death receptor–induced apoptosis through mutational inactivation of the proapoptotic Bcl-2 homolog Bax

LeBlanc, H. N., Lawrence, D. A., Varfolomeev, E. E., Tótpál, K., Morlan, J., Schow, P. W., Fong, S. E., SCHWALL, R. H., Sinicropi, D. V., & Ashkenazi, A. (2002) · Nature Medicine · doi:10.1038/nm0302-274 · Cited by 500 · see citing works

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 · see citing works

Structural Basis of Caspase Inhibition by XIAP

Huang, Y., Park, Y. C., Rich, R. L., Segal, D., Myszka, D. G., & Wu, H. (2001) · Cell · doi:10.1016/s0092-8674(01)00273-2 · Cited by 480 · see citing works

TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLOPreprint

Deng, Y., Lin, Y., & Wu, X. (2002) · Genes & Development · doi:10.1101/gad.949602 · Cited by 456 · see citing works

TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2

Li, X., Yang, Y., & Ashwell, J. D. (2002) · Nature · doi:10.1038/416345a · Cited by 452 · see citing works

Identification of XAF1 as an antagonist of XIAP anti-Caspase activity

Liston, P., Fong, W. G., Kelly, N. L., Toji, S., Miyazaki, T., Conte, D., Tamai, K., Craig, C. G., McBurney, M. W., & Korneluk, R. G. (2001) · Nature Cell Biology · doi:10.1038/35055027 · Cited by 441 · see citing works

Characterization of XIAP-Deficient Mice

Harlin, H., Reffey, S. B., Duckett, C. S., Lindsten, T., & Thompson, C. B. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3604-3608.2001 · Cited by 422 · see citing works

Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains

Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V. (1999) · Science · doi:10.1126/science.283.5401.543 · Cited by 415 · see citing works

ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas

Vucic, D., Stennicke, H. R., Pisabarro, M. T., Salvesen, G. S., & Dixit, V. M. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00781-8 · Cited by 413 · see citing works

Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

Krojer, T. J., Garrido-Franco, M., Huber, R., Ehrmann, M., & Clausen, T. (2002) · Nature · doi:10.1038/416455a · Cited by 403 · see citing works

Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosisPreprint

Grumont, R. J., Rourke, I. J., & Gerondakis, S. (1999) · Genes & Development · doi:10.1101/gad.13.4.400 · Cited by 403 · see citing works

Casper Is a FADD- and Caspase-Related Inducer of Apoptosis

Shu, H., Halpin, D. R., & Goeddel, D. V. (1997) · Immunity · doi:10.1016/s1074-7613(00)80450-1 · Cited by 399 · see citing works

XIAP, a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1–TAK1 in the BMP signaling pathway

Yamaguchi, K., Nagai, S., Ninomiya‐Tsuji, J., Nishita, M., Tamai, K., Irie, K., Ueno, N., Nishida, E., Shibuya, H., & Matsumoto, K. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.179 · Cited by 395 · see citing works

XIAP: Apoptotic brake and promising therapeutic target

Holčı́k, M., Gibson, H. D. F., & Korneluk, R. G. (2001) · APOPTOSIS · doi:10.1023/a:1011379307472 · Cited by 385 · see citing works

Apoptosis Induction by Caspase-8 Is Amplified through the Mitochondrial Release of Cytochrome c

Kuwana, T., Smith, J. J., Muzio, M., Dixit, V. M., Newmeyer, D. D., & Kornbluth, S. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16589 · Cited by 376 · see citing works

I-FLICE, a Novel Inhibitor of Tumor Necrosis Factor Receptor-1- and CD-95-induced Apoptosis

Hu, S., Vincenz, C., Ni, J., Gentz, R., & Dixit, V. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17255 · Cited by 375 · see citing works

Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms

Yoo, S. J., Huh, J. R., Muro, I., Yu, H., Wang, L., Wang, S. L., Feldman, R. M. R., Clem, R. J., Müller, H. ‐. J., & Hay, B. A. (2002) · Nature Cell Biology · doi:10.1038/ncb793 · Cited by 373 · see citing works

Properties of the caspases

Stennicke, H. R., & Salvesen, G. S. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00133-2 · Cited by 373 · see citing works

An exegesis of IAPs: salvation and surprises from BIR motifs

Miller, L. K. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01609-8 · Cited by 370 · see citing works

Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs.

Verhagen, A. M., Coulson, E. J., & Vaux, D. L. (2001) · Genome biology · doi:10.1186/gb-2001-2-7-reviews3009 · Cited by 363 · see citing works

The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity

Loo, G., van Gurp, M., Depuydt, B., Srinivasula, S. M., Rodríguez, I., Alnemri, E. S., Gevaert, K., Vandekerckhove, J. S., Declercq, W., & Vandenabeele, P. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400970 · Cited by 357 · see citing works

The Inhibitor of Apoptosis, cIAP2, Functions as a Ubiquitin-Protein Ligase and Promotes in VitroMonoubiquitination of Caspases 3 and 7

Huang, H.-K., Joazeiro, C. A. P., Bonfoco, E., Kamada, S., Leverson, J. D., & Hunter, T. R. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61427-4 · Cited by 356 · see citing works

Molecular Determinants of the Caspase-promoting Activity of Smac/DIABLO and Its Role in the Death Receptor Pathway

Srinivasula, S. M., Datta, P., Fan, X., Fernandes‐Alnemri, T., Huang, Z., & Alnemri, E. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000533200 · Cited by 354 · see citing works

NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP

Sun, C. C., Cai, M., Gunasekera, A. H., Meadows, R. P., Wang, H., Chen, J., Zhang, H., Wu, W., Xu, N., Ng, S., et al. (1999) · Nature · doi:10.1038/44617 · Cited by 343 · see citing works

FLAME-1, a Novel FADD-like Anti-apoptotic Molecule That Regulates Fas/TNFR1-induced Apoptosis

Srinivasula, S. M., Ahmad, M., Ottilie, S., Bullrich, F., Banks, S., Wang, Y., Fernandes‐Alnemri, T., Croce, C. M., Litwack, G., Tomaselli, K. J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18542 · Cited by 335 · see citing works

The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7.

Huang, H.-K., Joazeiro, C. A. P., Bonfoco, E., et al. (2000) · PubMed · doi:10.1074/jbc.c000199200 · Cited by 333 · see citing works

Apaf-1 Oligomerizes into Biologically Active ∼700-kDa and Inactive ∼1.4-MDa Apoptosome Complexes

Cain, K., Bratton, S. B., Langlais, C., Walker, G. R., Brown, D. G., Sun, X.-M., & Cohen, G. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6067 · Cited by 321 · see citing works

CASH, a Novel Caspase Homologue with Death Effector Domains

Goltsev, Y. V., Kovalenko, A., Arnold, E., Varfolomeev, E. E., Brodianskii, V. M., & Wallach, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19641 · Cited by 318 · see citing works

Cell death attenuation by `Usurpin', a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex

Rasper, D., Vaillancourt, J. P., Hadano, S., Houtzager, V. M., Seiden, I. M., Keen, S., Tawa, P., Xanthoudakis, S., Nasir, J., Martindale, D. W., et al. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400370 · Cited by 316 · see citing works

CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis

Inohara, N., Koseki, T., Hu, Y., Chen, S., & Núñez, G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10717 · Cited by 315 · see citing works

A structural view of mitochondria-mediated apoptosis.

Shi, Y. (2001) · Nature Structural Biology · doi:10.1038/87548 · Cited by 307 · see citing works

A new internal-ribosome-entry-site motif potentiates XIAP- mediated cytoprotection

Holčı́k, M., Lefebvre, C. A., Yeh, C., Chow, T. Y.-K., & Korneluk, R. G. (1999) · Nature Cell Biology · doi:10.1038/11109 · Cited by 302 · see citing works

Caspase Activation Involves the Formation of the Aposome, a Large (∼700 kDa) Caspase-activating Complex

Cain, K., Brown, D. G., Langlais, C., & Cohen, G. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22686 · Cited by 301 · see citing works

The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis

Wilson, R., Goyal, L., Ditzel, M., Zachariou, A., Baker, D. A., Agapite, J., Steller, H., & Meier, P. (2002) · Nature Cell Biology · doi:10.1038/ncb799 · Cited by 296 · see citing works

Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1

Ryoo, H. D., Bergmann, A., Gonen, H., Ciechanover, A. J., & Steller, H. (2002) · Nature Cell Biology · doi:10.1038/ncb795 · Cited by 278 · see citing works

Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi

Li, W., Srinivasula, S. M., Chai, J., Li, P., Wu, J., Zhang, Z., Alnemri, E. S., & Shi, Y. (2002) · Nature Structural Biology · doi:10.1038/nsb795 · Cited by 277 · see citing works

Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death

Holčı́k, M., Yeh, C., Korneluk, R. G., & Chow, T. Y.-K. (2000) · Oncogene · doi:10.1038/sj.onc.1203765 · Cited by 258 · see citing works

NMR Structure and Mutagenesis of the Third Bir Domain of the Inhibitor of Apoptosis Protein XIAP

Sun, C. C., Cai, M., Meadows, R. P., Xu, N., Gunasekera, A. H., Herrmann, J. E., Wu, J. C., & Fesik, S. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006226200 · Cited by 254 · see citing works

The Survivin-like C. elegans BIR-1 Protein Acts with the Aurora-like Kinase AIR-2 to Affect Chromosomes and the Spindle Midzone

Speliotes, E. K., Uren, A. G., Vaux, D. L., & Horvitz, H. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00023-x · Cited by 244 · see citing works

Internal ribosome initiation of translation and the control of cell death

Holčı́k, M., Sonenberg, N., & Korneluk, R. G. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02106-5 · Cited by 239 · see citing works

Bcl-2 and Bcl-xL Inhibit CD95-mediated Apoptosis by Preventing Mitochondrial Release of Smac/DIABLO and Subsequent Inactivation of X-linked Inhibitor-of-Apoptosis Protein

Sun, X.-M., Bratton, S. B., Butterworth, M., MacFarlane, M., & Cohen, G. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109893200 · Cited by 237 · see citing works

MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclX L and initiates cell death

Han, D. K. M., Chaudhary, P. M., Wright, M. E., Friedman, C. L., Trask, B. J., Riedel, R. T., Baskin, D., Schwartz, S. M., & Hood, L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11333 · Cited by 235 · see citing works

Structural Basis of Caspase Inhibition by XIAP Differential Roles of the Linker versus the BIR Domain

Huang, Y. (2001) · Cell · doi:10.1016/s0092-8674(02)02075-5 · Cited by 233 · see citing works

Translation initiation factor modifications and the regulation of protein synthesis in apoptotic cells

Clemens, M. J., Bushell, M., Jeffrey, I. W., Pain, V. M., & Morley, S. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400695 · Cited by 228 · see citing works

Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis

Fraser, A. G., James, C., Evan, G. I., & Hengartner, M. O. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80137-7 · Cited by 224 · see citing works

Human IAP-Like Protein Regulates Programmed Cell Death Downstream of Bcl-x L and Cytochrome c

Duckett, C. S., Li, F., Wang, Y., Tomaselli, K. J., Thompson, C. B., & Armstrong, R. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.608 · Cited by 217 · see citing works

IAP Suppression of Apoptosis Involves Distinct Mechanisms: the TAK1/JNK1 Signaling Cascade and Caspase Inhibition

Sanna, M. G., Correia, J. D. S., Ducrey, O., Lee, J., Nomoto, K., Schrantz, N., Deveraux, Q. L., & Ulevitch, R. J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1754-1766.2002 · Cited by 217 · see citing works

Identification of cIAP1 as a candidate target gene within an amplicon at 11q22 in esophageal squamous cell carcinomas.

Imoto, I., Yang, Z.-Q., Pimkhaokham, A., Tsuda, H., Shimada, Y., Imamura, M., Ohki, M., & Inazawa, J. (2001) · PubMed · Cited by 213 · see citing works

Expression and Genetic Analysis of XIAP-Associated Factor 1 (XAF1) in Cancer Cell Lines

Fong, W. G., Liston, P., Rajcan‐Separovic, E., Jean, M. S., Craig, C. G., & Korneluk, R. G. (2000) · Genomics · doi:10.1006/geno.2000.6364 · Cited by 213 · see citing works

Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

Holley, C. L., Olson, M. R., Colón‐Ramos, D. A., & Kornbluth, S. A. (2002) · Nature Cell Biology · doi:10.1038/ncb798 · Cited by 203 · see citing works

Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts

Uren, A. G., Coulson, E. J., & Vaux, D. L. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01198-0 · Cited by 202 · see citing works

Tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of human melanoma is regulated by smac/DIABLO release from mitochondria.

Zhang, X. D., Zhang, X., Gray, C. P., Nguyen, T., & Hersey, P. (2001) · PubMed · Cited by 200 · see citing works

New Ways of Initiating Translation in Eukaryotes?

Kozak, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.1899-1907.2001 · Cited by 194 · see citing works

Role for yeast inhibitor of apoptosis (IAP)-like proteins in cell division

Uren, A. G., Beilharz, T. H., O’Connell, M. J., Bugg, S. J., van Driel, R. R., Vaux, D. L., & Lithgow, T. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10170 · Cited by 191 · see citing works

The Neuronal Apoptosis Inhibitory Protein Is a Direct Inhibitor of Caspases 3 and 7

Maier, J. K. X., Lahoua, Z., Gendron, N. H., Fetni, R., Johnston, A., Davoodi, J., Rasper, D., Roy, S., Slack, R. S., Nicholson, D. W., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-06-02035.2002 · Cited by 185 · see citing works

Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat.

Day, C. L., Hinds, M. G., Norton, R. S., & Vaux, D. L. (1999) · Nature Structural Biology · doi:10.1038/10701 · Cited by 182 · see citing works

Controlling the Caspases

Fesik, S. W., & Shi, Y. (2001) · Science · doi:10.1126/science.1062236 · Cited by 173 · see citing works

Reprieval from execution: the molecular basis of caspase inhibition

Stennicke, H. R., Ryan, C., & Salvesen, G. S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02045-x · Cited by 162 · see citing works

SMAC Negatively Regulates the Anti-apoptotic Activity of Melanoma Inhibitor of Apoptosis (ML-IAP)

Vucic, D., Deshayes, K., Ackerly, H., Pisabarro, M. T., Kadkhodayan, S., Fairbrother, W. J., & Dixit, V. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112045200 · Cited by 162 · see citing works

Identification of a candidate modifying gene for spinal muscular atrophy by comparative genomics

Scharf, J. M., Endrizzi, M. G., Wetter, A., Huang, S., Thompson, T. G., Zerres, K., Dietrich, W. F., Wirth, B., & Kunkel, L. M. (1998) · Nature Genetics · doi:10.1038/1753 · Cited by 154 · see citing works

BIRinging Chromosomes through Cell Division—And Survivin' the Experience

Reed, J. C., & Bischoff, J. R. (2000) · Cell · doi:10.1016/s0092-8674(00)00076-3 · Cited by 151 · see citing works

X-linked Inhibitor of Apoptosis Protein Functions as a Cofactor in Transforming Growth Factor-β Signaling

Reffey, S. B., Würthner, J., Parks, W. T., Roberts, A. B., & Duckett, C. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100331200 · Cited by 147 · see citing works

xIAP Induces Cell-Cycle Arrest and Activates Nuclear Factor-κB

Levkau, B., Garton, K. J., Ferri, N., Kloke, K., Nofer, J., Baba, H. A., Raines, E. W., & BREITHARDT, G. E. (2001) · Circulation Research · doi:10.1161/01.res.88.3.282 · Cited by 137 · see citing works

The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3– and caspase 9–interacting sites

Silke, J., Hawkins, C. J., Ekert, P. G., Chew, J., Day, C. L., Pakusch, M., Verhagen, A. M., & Vaux, D. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108085 · Cited by 133 · see citing works

sickle, a Novel Drosophila Death Gene in the reaper/hid/grim Region, Encodes an IAP-Inhibitory Protein

Srinivasula, S. M., Datta, P., Kobayashi, M., Wu, J.-W., Fujioka, M., Hegde, R. P., Zhang, Z., Mukattash, R., Fernandes‐Alnemri, T., Shi, Y., et al. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00657-1 · Cited by 131 · see citing works

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP

Sanna, M. G., Duckett, C. S., Richter, B. W. M., Thompson, C. B., & Ulevitch, R. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6015 · Cited by 129 · see citing works

The Damage-Responsive Drosophila Gene sickle Encodes a Novel IAP Binding Protein Similar to but Distinct from reaper, grim, and hid

Christich, A., Kauppila, S., Chen, P., Sogame, N., Ho, S. I., & Abrams, J. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00658-3 · Cited by 125 · see citing works

Drosophila Morgue is an F box/ubiquitin conjugase domain protein important for grim-reaper mediated apoptosis

Wing, J. P., Schreader, B. A., Yokokura, T., Wang, Y., Andrews, P. S., Huseinovic, N., Dong, C. K., Ogdahl, J. L., Schwartz, L. M., White, K., et al. (2002) · Nature Cell Biology · doi:10.1038/ncb800 · Cited by 123 · see citing works

Direct inhibition of caspase 3 is dispensable for the anti‐apoptotic activity of XIAP

Silke, J., Ekert, P. G., Day, C. L., Hawkins, C. J., Baca, M., Chew, J., Pakusch, M., Verhagen, A. M., & Vaux, D. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3114 · Cited by 122 · see citing works

Morgue mediates apoptosis in the Drosophila melanogaster retina by promoting degradation of DIAP1

Hays, R., Wickline, L., & Cagan, R. L. (2002) · Nature Cell Biology · doi:10.1038/ncb794 · Cited by 121 · see citing works

Two kinds of BIR-containing protein - inhibitors of apoptosis, or required for mitosis

Silke, J., & Vaux, D. L. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.10.1821 · Cited by 121 · see citing works

Structural Analysis of a Functional DIAP1 Fragment Bound to Grim and Hid Peptides

Wu, J.-W., Cocina, A. E., Chai, J., Hay, B. A., & Shi, Y. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00282-9 · Cited by 121 · see citing works

Participation of Bir1p, a member of the inhibitor of apoptosis family, in yeast chromosome segregation events

Yoon, H., & Carbon, J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13208 · Cited by 120 · see citing works

Drosophila sickle Is a Novel grim-reaper Cell Death Activator

Wing, J. P., Karres, J. S., Ogdahl, J. L., Zhou, L. J., Schwartz, L. M., & Nambu, J. R. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00664-9 · Cited by 117 · see citing works

Erratum: correction: A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

Srinivasula, S. M., Hegde, R. P., Saleh, A., Datta, P., Shiozaki, E. N., Chai, J., Lee, R., Robbins, P. D., Fernandes‐Alnemri, T., Shi, Y., et al. (2001) · Nature · doi:10.1038/35082622 · Cited by 115 · see citing works

c-IAP1 Is Cleaved by Caspases to Produce a Proapoptotic C-terminal Fragment

Clem, R. J., Sheu, T.-T., Richter, B. W. M., He, W.-W., Thornberry, N. A., Duckett, C. S., & Hardwick, J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010259200 · Cited by 107 · see citing works

The Inhibitor of Apoptosis Protein-Binding Domain of Smac Is Not Essential for Its Proapoptotic Activity

Roberts, D. L., Merrison, W., MacFarlane, M., & Cohen, G. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.1.221 · Cited by 102 · see citing works

Distinct cell killing properties of the Drosophila reaper, head involution defective, and grim genes

Wing, J. P., Zhou, L., Schwartz, L. M., & Nambu, J. R. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400423 · Cited by 100 · see citing works

Molecular Cloning of ILP-2, a Novel Member of the Inhibitor of Apoptosis Protein Family

Richter, B. W. M., Mir, S. S., Eiben, L. J., Lewis, J., Reffey, S. B., Frattini, A., Tian, L., Frank, S., Youle, R. J., Nelson, D. L., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4292-4301.2001 · Cited by 100 · see citing works

Biochemical and Genetic Interactions betweenDrosophila Caspases and the Proapoptotic Genesrpr, hid, and grim

Song, Z., Guan, B., Bergman, A., Nicholson, D. W., Thornberry, N. A., Peterson, E. P., & Steller, H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2907-2914.2000 · Cited by 99 · see citing works

The hippocampal neurons of neuronal apoptosis inhibitory protein 1 (NAIP1)-deleted mice display increased vulnerability to kainic acid-induced injury

Holčı́k, M., Thompson, C. S., Yaraghi, Z., Lefebvre, C. A., MacKenzie, A., & Korneluk, R. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040469797 · Cited by 96 · see citing works

Neurotrophin Receptor-interacting Mage Homologue Is an Inducible Inhibitor of Apoptosis Protein-interacting Protein That Augments Cell Death

Jordan, B. W. M., Dinev, D., Mellay, V. L., Troppmair, J., Götz, R., Wixler, L., Sendtner, M., Ludwig, S., & Rapp, U. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100171200 · Cited by 93 · see citing works

The RHG motifs of Drosophila Reaper and Grim are important for their distinct cell death-inducing abilities

Wing, J. P., Schwartz, L. M., & Nambu, J. R. (2001) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00316-1 · Cited by 66 · see citing works

Genomic Sequence Analysis of the Mouse Naip Gene ArrayPreprint

Endrizzi, M. G., Hadinoto, V., Growney, J. D., Miller, W., & Dietrich, W. F. (2000) · Genome Research · doi:10.1101/gr.10.8.1095 · Cited by 64 · see citing works

Thymocyte-targeted overexpression of xiap transgene disrupts T lymphoid apoptosis and maturation

Conte, D., Liston, P., Wong, J. W. W., Wright, K. E., & Korneluk, R. G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081547998 · Cited by 60 · see citing works

New Ways of Initiating Translation in Eukaryotes?

Schneider, R. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8238-8246.2001 · Cited by 57 · see citing works

Molecular mechanisms of cell death and phagocytosis in Drosophila

Bangs, P. L., Franc, N. C., & White, K. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400754 · Cited by 45 · see citing works

Schizosaccharomyces pombe Bir1p, a Nuclear Protein That Localizes to Kinetochores and the Spindle Midzone, Is Essential for Chromosome Condensation and Spindle Elongation During Mitosis

Rajagopalan, S., & Balasubramanian, M. K. (2002) · Genetics · doi:10.1093/genetics/160.2.445 · Cited by 40 · see citing works

Sequence Requirements for Hid Binding and Apoptosis Regulation in the Baculovirus Inhibitor of Apoptosis Op-IAP

Wright, C. W., & Clem, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110500200 · Cited by 39 · see citing works

Ubiquitin biology: an old dog learns an old trick

Pickart, C. M. (2000) · Nature Cell Biology · doi:10.1038/35019610 · Cited by 19 · see citing works

Inhibitor of Apoptosis Protein from Orgyia pseudotsugata Nuclear Polyhedrosis Virus Provides a Costimulatory Signal Required for Optimal Proliferation of Developing Thymocytes

Robles, M. S., Leonardo, E., Criado, L. M., Izquierdo, M., & Martínez‐A, C. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.4.1770 · Cited by 10 · 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 &amp; Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Smad-dependent and Smad-independent pathways in TGF-β family signalling

Derynck, R., & Zhang, Y. E. (2003) · Nature · doi:10.1038/nature02006 · Cited by 5,370 · see citing works

Cell Death

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

Robbins and Cotran Pathologic Basis of Disease

Hoda, S. A., & Hoda, R. S. (2020) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqaa163 · Cited by 3,369 · see citing works

The integrated stress response

Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659 · see citing works

Molecular mechanisms of caspase regulation during apoptosis

Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,893 · see citing works

Metastasis: a question of life or death

Mehlen, P., & Puisieux, A. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1886 · Cited by 1,854 · see citing works

Molecular mechanisms of drug resistance

Longley, D., & Johnston, P. (2005) · The Journal of Pathology · doi:10.1002/path.1706 · Cited by 1,686 · see citing works

Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies

Pistritto, G., Trisciuoglio, D., Ceci, C., Garufi, A., & D’Orazi, G. (2016) · Aging · doi:10.18632/aging.100934 · Cited by 1,670 · see citing works

IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis

Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works

Validating survivin as a cancer therapeutic target

Altieri, D. C. (2003) · Nature reviews. Cancer · doi:10.1038/nrc968 · Cited by 1,204 · see citing works

cIAP1 and cIAP2 Facilitate Cancer Cell Survival by Functioning as E3 Ligases that Promote RIP1 Ubiquitination

Bertrand, M. J. M., Milutinovic, S., Dickson, K. M., Ho, W. C., Boudreault, A., Durkin, J. P., Gillard, J. W., Jaquith, J. B., Morris, S. J., & Barker, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.014 · Cited by 1,102 · see citing works

Identification and validation of oncogenes in liver cancer using an integrative oncogenomic approach

Zender, L., Spector, M. S., Xue, W., Flemming, P., Cordon-Cardo, C., Silke, J., Fan, S.-T., Luk, J. M., Wigler, M., Hannon, G. J., et al. (2006) · Cell · doi:10.1016/j.cell.2006.05.030 · Cited by 1,065 · see citing works

Toxic proteins released from mitochondria in cell death

Saelens, X., Festjens, N., Walle, L. V., van Gurp, M., Loo, G., & Vandenabeele, P. (2004) · Oncogene · doi:10.1038/sj.onc.1207523 · Cited by 977 · see citing works

Role of Bcl-2 family proteins and caspases in the regulation of apoptosis

Ola, M. S., Nawaz, M. I., & Ahsan, H. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0709-x · Cited by 916 · see citing works

Survivin, versatile modulation of cell division and apoptosis in cancer

Altieri, D. C. (2003) · Oncogene · doi:10.1038/sj.onc.1207113 · Cited by 899 · see citing works

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works

The protein structures that shape caspase activity, specificity, activation and inhibition

Fuentes‐Prior, P., & Salvesen, G. S. (2004) · Biochemical Journal · doi:10.1042/bj20041142 · Cited by 877 · see citing works

Targeting IAP proteins for therapeutic intervention in cancer

Fulda, S., & Vucic, D. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3627 · Cited by 837 · see citing works

Apoptosis and melanoma chemoresistance

Soengas, M. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1206454 · Cited by 822 · see citing works

Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family

Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813 · see citing works

Survivin: Key Regulator of Mitosis and Apoptosis and Novel Target for Cancer Therapeutics

Mita, A. C., Mita, M. M., Nawrocki, S. T., & Giles, F. J. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0746 · Cited by 760 · see citing works

NALPs: a novel protein family involved in inflammation

Tschopp, J., Martinon, F., & Burns, K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1019 · Cited by 719 · see citing works

Mechanism of XIAP-Mediated Inhibition of Caspase-9

Shiozaki, E. N., Chai, J., Rigotti, D. J., Riedl, S. J., Li, P., Srinivasula, S. M., Alnemri, E. S., Fairman, R., & Shi, Y. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00054-6 · Cited by 718 · see citing works

MicroRNAs: key players in the immune system, differentiation, tumorigenesis and cell death

Schickel, R., Boyerinas, B. M., Sm, P., & Peter, M. E. (2008) · Oncogene · doi:10.1038/onc.2008.274 · Cited by 713 · see citing works

Apoptosis and cancer: mutations within caspase genes

Ghavami, S., Hashemi, M. M., Ande, S. R., Yeganeh, B., Xiao, W., Eshraghi, M., Bus, C., Kadkhoda, K., Wiecheć, E., Halayko, A. J., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.066944 · Cited by 712 · see citing works

Molecular targets in cerebral ischemia for developing novel therapeutics

Mehta, S. L., Manhas, N., & Raghubir, R. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.11.003 · Cited by 707 · see citing works

XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome

Rigaud, S., Fondanèche, M., Lambert, N., Pasquier, B., Mateo, V., Soulas-Sprauel, P., Galicier, L., Deist, F. L., Rieux‐Laucat, F., Revy, P., et al. (2006) · Nature · doi:10.1038/nature05257 · Cited by 703 · see citing works

Molecular Circuits of Resolution: Formation and Actions of Resolvins and Protectins

Bannenberg, G. L., Chiang, N., Ariel, A., Arita, M., Tjonahen, E., Gotlinger, K. H., Hong, S., & Serhan, C. N. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.7.4345 · Cited by 699 · see citing works

Apoptosis and Necrosis in the Liver: A Tale of Two Deaths?

Malhi, H., Gores, G. J., & Lemasters, J. J. (2006) · Hepatology · doi:10.1002/hep.21062 · Cited by 688 · see citing works

`The stress of dying': the role of heat shock proteins in the regulation of apoptosis

Beere, H. M. (2004) · Journal of Cell Science · doi:10.1242/jcs.01284 · Cited by 638 · see citing works

IAPs, RINGs and ubiquitylation

Vaux, D. L., & Silke, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1621 · Cited by 611 · see citing works

Major apoptotic mechanisms and genes involved in apoptosis

Kiraz, Y., Adan, A., Yandım, M. K., & Baran, Y. (2016) · Tumor Biology · doi:10.1007/s13277-016-5035-9 · Cited by 585 · see citing works

Get a ligand, get a life: integrins, signaling and cell survival

Stupack, D. G., & Cheresh, D. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.00071 · Cited by 580 · see citing works

Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization

Nikolovska‐Coleska, Z., Wang, R., Fang, X., Pan, H., Tomita, Y. A., Li, P., Roller, P. P., Krajewski, K., Saito, N. G., Stuckey, J. A., et al. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.05.055 · Cited by 555 · see citing works

Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy

Almasan, A., & Ashkenazi, A. (2003) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(03)00029-7 · Cited by 547 · see citing works

Crosstalk of autophagy and apoptosis: Involvement of the dual role of autophagy under ER stress

Song, S., Tan, J., Miao, Y., Li, M., & Zhang, Q. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25785 · Cited by 524 · see citing works

Inhibitor of Apoptosis Proteins: Translating Basic Knowledge into Clinical Practice

Schimmer, A. D. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1918 · Cited by 513 · see citing works

Death receptors in chemotherapy and cancer

Debatin, K., & Krammer, P. H. (2004) · Oncogene · doi:10.1038/sj.onc.1207558 · Cited by 505 · see citing works

Tumor Necrosis Factor

Varfolomeev, E. E., & Ashkenazi, A. (2004) · Cell · doi:10.1016/s0092-8674(04)00166-7 · Cited by 498 · see citing works

Apoptosis—an introduction

Lawen, A. (2003) · BioEssays · doi:10.1002/bies.10329 · Cited by 493 · see citing works

Stress and Radiation-Induced Activation of Multiple Intracellular Signaling Pathways1

Dent, P., Yacoub, A., Contessa, J. N., Carón, R. W., Amorino, G. P., Valerie, K. C., Hagan, M. P., Grant, S., & Schmidt‐Ullrich, R. (2003) · Radiation Research · doi:10.1667/0033-7587(2003)159[0283:sariao]2.0.co;2 · Cited by 465 · see citing works

Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 451 · see citing works

Survivin: a unique target for tumor therapy

Garg, H., Suri, P., Gupta, J. C., Talwar, G. P., & Dubey, S. (2016) · Cancer Cell International · doi:10.1186/s12935-016-0326-1 · Cited by 442 · see citing works

Oncogene addiction: setting the stage for molecularly targeted cancer therapyPreprint

Sharma, S. V., & Settleman, J. E. (2007) · Genes & Development · doi:10.1101/gad.1609907 · Cited by 442 · see citing works

XIAP inhibits caspase‐3 and ‐7 using two binding sites: evolutionarily conserved mechanism of IAPs

Scott, F. L., Denault, J., Riedl, S. J., Shin, H., Renatus, M., & Salvesen, G. S. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600544 · Cited by 420 · see citing works

Caspase Activity and a Specific Cytochrome C Are Required for Sperm Differentiation in Drosophila

Arama, E., Agapite, J., & Steller, H. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00120-5 · Cited by 417 · see citing works

Mechanisms of temozolomide resistance in glioblastoma - a comprehensive review

Singh, N. C., Miner, A., Hennis, L., & Mittal, S. (2020) · Cancer Drug Resistance · doi:10.20517/cdr.2020.79 · Cited by 408 · see citing works

Protein Knockdown Using Methyl Bestatin−Ligand Hybrid Molecules: Design and Synthesis of Inducers of Ubiquitination-Mediated Degradation of Cellular Retinoic Acid-Binding Proteins

Itoh, Y., Ishikawa, M., Naito, M., & Hashimoto, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100691p · Cited by 404 · see citing works

How death shapes life during development

Baehrecke, E. H. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm931 · Cited by 402 · see citing works

Apoptosis-based therapies for hematologic malignancies

Reed, J. C., & Pellecchia, M. (2005) · Blood · doi:10.1182/blood-2004-07-2761 · Cited by 402 · see citing works

Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis

Dohi, T., Beltrami, E., Wall, N. R., Plescia, J., & Altieri, D. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22222 · Cited by 401 · see citing works

An IAP-IAP Complex Inhibits Apoptosis

Dohi, T., Okada, K., Xia, F., Wilford, C. E., Samuel, T., Welsh, K., Marusawa, H., Zou, H., Armstrong, R., Matsuzawa, S.-I., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400236200 · Cited by 400 · see citing works

The Human Anti-apoptotic Proteins cIAP1 and cIAP2 Bind but Do Not Inhibit Caspases

Eckelman, B. P., & Salvesen, G. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510863200 · Cited by 391 · see citing works

Apoptosis and Necrosis in the Liver

Guicciardi, M. E., Malhi, H., Mott, J. L., & Gores, G. J. (2013) · Comprehensive physiology · doi:10.1002/cphy.c120020 · Cited by 387 · see citing works

Functional characterization of mitochondria in neutrophils: a role restricted to apoptosis

Mayanskiy, N. A., Geissler, J., Srinivasula, S. M., Alnemri, E. S., Roos, D., & Kuijpers, T. W. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401320 · Cited by 385 · see citing works

Apoptosis in the development and treatment of cancer

Gerl, R. E. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh283 · Cited by 385 · see citing works

Antisense therapy for cancer

Gleave, M. E., & Monia, B. P. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1631 · Cited by 380 · see citing works

Neuroprotection and acute spinal cord injury: A reappraisal

Hall, E. D., & Springer, J. E. (2004) · NeuroRx · doi:10.1602/neurorx.1.1.80 · Cited by 380 · see citing works

Survivin: A new target for anti-cancer therapy

Ryan, B. M., O’Donovan, N., & Duffy, M. J. (2009) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2009.05.003 · Cited by 378 · see citing works

Survivin and IAP proteins in cell-death mechanisms

Altieri, D. C. (2010) · Biochemical Journal · doi:10.1042/bj20100814 · Cited by 376 · see citing works

Apoptosis Deregulation and the Development of Cancer Multi-Drug Resistance

Neophytou, C. M., Trougakos, I. P., Erin, N., & Papageorgis, P. (2021) · Cancers · doi:10.3390/cancers13174363 · Cited by 376 · see citing works

Caspases — An update

Chowdhury, I., Tharakan, B., & Bhat, G. K. (2008) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2008.05.010 · Cited by 374 · see citing works

Gene therapy targeting survivin selectively induces pulmonary vascular apoptosis and reverses pulmonary arterial hypertension

McMurtry, M. S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23203 · Cited by 362 · see citing works

Caspase activation, inhibition, and reactivation: A mechanistic view

Shi, Y. (2004) · Protein Science · doi:10.1110/ps.04789804 · Cited by 361 · see citing works

Evolving Concepts of Apoptosis in Idiopathic Pulmonary Fibrosis

Thannickal, V. J., & Horowitz, J. C. (2006) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200601-001tk · Cited by 361 · see citing works

Downregulation of Bcl-2, FLIP or IAPs (XIAP and survivin) by siRNAs sensitizes resistant melanoma cells to Apo2L/TRAIL-induced apoptosis

Chawla‐Sarkar, M., Bae, S., Reu, F. J., Jacobs, B., Lindner, D. J., & Borden, E. C. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401416 · Cited by 359 · see citing works

Autophagic degradation of active caspase-8

Hou, W., Han, J., Lu, C., Goldstein, L. A., & Rabinowich, H. (2010) · Autophagy · doi:10.4161/auto.6.7.13038 · Cited by 356 · see citing works

New insights into apoptosis signaling by Apo2L/TRAIL

Gonzalvez, F., & Ashkenazi, A. (2010) · Oncogene · doi:10.1038/onc.2010.221 · Cited by 354 · see citing works

Neutrophil apoptosis pathways and their modifications in inflammation

Simon, H. (2003) · Immunological Reviews · doi:10.1034/j.1600-065x.2003.00038.x · Cited by 350 · see citing works

c‐IAP1 and UbcH5 promote K11‐linked polyubiquitination of RIP1 in TNF signalling

Dynek, J. N., Goncharov, T., Dueber, E. C., Fedorova, A. V., Izrael-Tomasevic, A., Phu, L., Helgason, E., Fairbrother, W. J., Deshayes, K., Kirkpatrick, D. S., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.300 · Cited by 350 · see citing works

Compensatory Proliferation Induced by Cell Death in the Drosophila Wing Disc Requires Activity of the Apical Cell Death Caspase Dronc in a Nonapoptotic Role

Huh, J. R., Guo, M., & Hay, B. A. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.015 · Cited by 349 · see citing works

Discovery of Embelin as a Cell-Permeable, Small-Molecular Weight Inhibitor of XIAP through Structure-Based Computational Screening of a Traditional Herbal Medicine Three-Dimensional Structure Database

Nikolovska‐Coleska, Z., Xu, L., Hu, Z., Tomita, Y. A., Li, P., Roller, P. P., Wang, R., Fang, X., Guo, R., Zhang, M., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030420+ · Cited by 345 · see citing works

Betulinic Acid for Cancer Treatment and Prevention

Fulda, S. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9061096 · Cited by 344 · see citing works

Cellular Inhibitors of Apoptosis cIAP1 and cIAP2 Are Required for Innate Immunity Signaling by the Pattern Recognition Receptors NOD1 and NOD2

Bertrand, M. J. M., Doiron, K., Labbè, K., Korneluk, R. G., Barker, P. A., & Saleh, M. (2009) · Immunity · doi:10.1016/j.immuni.2009.04.011 · Cited by 338 · see citing works

siRNA targeting of the viral E6 oncogene efficiently kills human papillomavirus-positive cancer cells

Butz, K., Ristriani, T., Hengstermann, A., Denk, C., Scheffner, M., & Hoppe‐Seyler, F. (2003) · Oncogene · doi:10.1038/sj.onc.1206894 · Cited by 335 · see citing works

Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosisPreprint

Yang, Q.-H., Church-Hajduk, R., Ren, J., Newton, M. L., & Du, C. (2003) · Genes & Development · doi:10.1101/gad.1097903 · Cited by 332 · see citing works

Inhibitor of Apoptosis (IAP) Proteins-Modulators of Cell Death and InflammationPreprint

Silke, J., & Meier, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008730 · Cited by 329 · see citing works

Apoptosis, Stem Cells, and Tissue Regeneration

Bergmann, A., & Steller, H. (2010) · Science Signaling · doi:10.1126/scisignal.3145re8 · Cited by 325 · see citing works

Survivin and molecular pathogenesis of colorectal cancer

Kim, P. J., Plescia, J., Clevers, H. C., Fearon, E. R., & Altieri, D. C. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13910-4 · Cited by 322 · see citing works

Critical Role of Endogenous Akt/IAPs and MEK1/ERK Pathways in Counteracting Endoplasmic Reticulum Stress-induced Cell Death

Hu, P., Han, Z., Couvillon, A. D., & Exton, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407700200 · Cited by 318 · see citing works

Regulation of survivin function by Hsp90

Fortugno, P., Beltrami, E., Plescia, J., Fontana, J. T., Pradhan, D., Marchisio, P. C., Sessa, W. C., & Altieri, D. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2434345100 · Cited by 316 · see citing works

Caspases: Keys in the Ignition of Cell Death

Denault, J., & Salvesen, G. S. (2002) · Chemical Reviews · doi:10.1021/cr010183n · Cited by 314 · see citing works

Bistability Analyses of a Caspase Activation Model for Receptor-induced Apoptosis

Eißing, T., Conzelmann, H., Gilles, E. D., Allgöwer, F., Bullinger, E., & Scheurich, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404893200 · Cited by 313 · see citing works

Mathematical modeling reveals threshold mechanism in CD95-induced apoptosis

Bentele, M., Lavrik, I. N., Ulrich, M., Stößer, S., Heermann, D. W., Kalthoff, H., Krammer, P. H., & Eils, R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404158 · Cited by 311 · see citing works

Survivin study: What is the next wave?

Li, F. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10327 · Cited by 311 · see citing works

Chemosensitization of tumors by resveratrol

Gupta, S. C., Kannappan, R., Reuter, S., Kim, J. H., & Aggarwal, B. B. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05852.x · Cited by 308 · see citing works

Hsp60 Regulation of Tumor Cell Apoptosis

Ghosh, J. C., Dohi, T., Kang, B. H., & Altieri, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705904200 · Cited by 307 · see citing works

The Role of Apoptosis in the Regulation of Trophoblast Survival and Differentiation during Pregnancy

Chavez, S. L., Abrahams, V. M., & Mor, G. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0003 · Cited by 305 · see citing works

Death without caspases, caspases without death

Abraham, M. C., & Shaham, S. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.03.002 · Cited by 302 · see citing works

Apoptotic and non-apoptotic programmed cardiomyocyte death in ventricular remodelling

Dorn, G. W. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn243 · Cited by 301 · see citing works

Survival signalling and apoptosis resistance in glioblastomas: opportunities for targeted therapeutics

Krakstad, C., & Chekenya, M. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-135 · Cited by 301 · see citing works

The Apoptosome Activates Caspase-9 by Dimerization

Pop, C., Timmer, J. C., Sperandio, S., & Salvesen, G. S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.009 · Cited by 294 · see citing works

Endogenous Reactive Intermediates as Modulators of Cell Signaling and Cell Death

West, J. D., & Marnett, L. J. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050321u · Cited by 293 · see citing works

Regulation of Human Neutrophil Apoptosis and Lifespan in Health and Disease

McCracken, J., & Allen, L. H. (2014) · Journal of Cell Death · doi:10.4137/jcd.s11038 · Cited by 292 · see citing works

Programmed cell deaths

Guimarães, C. A., & Linden, R. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04084.x · Cited by 290 · see citing works

The case for survivin as a regulator of microtubule dynamics and cell-death decisions

Altieri, D. C. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.08.015 · Cited by 285 · see citing works

Apoptosis-based therapies and drug targets

Fischer, U., & Schulze‐Osthoff, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401556 · Cited by 280 · see citing works

Chemosensitization and Radiosensitization of Tumors by Plant Polyphenols

Garg, A. K., Buchholz, T. A., & Aggarwal, B. B. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1630 · Cited by 277 · see citing works

A Potent and Orally Active Antagonist (SM-406/AT-406) of Multiple Inhibitor of Apoptosis Proteins (IAPs) in Clinical Development for Cancer Treatment

Cai, Q., Sun, H., Peng, Y., Lü, J., Nikolovska‐Coleska, Z., McEachern, D., Liu, L., Qiu, S., Yang, C., Miller, R. S., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101505d · Cited by 274 · see citing works

Inhibitors of Apoptosis Proteins in Injury and Disease

Lotocki, G., & Keane, R. W. (2002) · IUBMB Life · doi:10.1080/15216540215675 · Cited by 23 · see citing works

The iap genes: unique arbitrators of cell death

Clem, R. J., & Duckett, C. S. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01088-x · Cited by 95 · see citing works

Inhibitor of Apoptosis Proteins

Garrison, J. B., Krieg, A. H., Welsh, K., Wen, Y., & Reed, J. C. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9780511976094.002 · Cited by 3 · see citing works

IAP family proteins---suppressors of apoptosisPreprint

Deveraux, Q. L., & Reed, J. C. (1999) · Genes & Development · doi:10.1101/gad.13.3.239 · Cited by 2,535 · see citing works

Advances in studies on inhibitor of apoptosis proteins

Li, J. (2005) · Anhui Medical and Pharmaceutical Journal