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

Apoptosis in the Pathogenesis and Treatment of Disease

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

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

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

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

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

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 3,174

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

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

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

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 2,577

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

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

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

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

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

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

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

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

Mechanisms of Caspase Activation and Inhibition during Apoptosis

Shi, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00482-3 · Cited by 1,850

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 1,735

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 1,562

Themes and variations on ubiquitylation

Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507

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 1,403

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

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

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 1,253

RING Finger Proteins

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

Protein regulation by monoubiquitin

Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227

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

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 1,140

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 1,079

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 1,019

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

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 989

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

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 965

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 943

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

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 872

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

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

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

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

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

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

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

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 736

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

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

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 675

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

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

Nuclear Factor (NF)-κB–regulated X-chromosome–linked iap 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 635

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

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 609

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

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 593

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

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

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

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 546

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

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

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

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 517

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

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

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

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 479

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 459

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 364

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

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 362

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

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

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

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

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

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 322

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

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

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 316

A structural view of mitochondria-mediated apoptosis.

Shi, Y. (2001) · Nature Structural Biology · doi:10.1038/87548 · Cited by 304

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

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

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

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

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

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 262

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

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

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

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 237

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

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 235

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

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

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 219

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 216

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

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

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

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

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

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

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

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

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

Controlling the Caspases

Fesik, S. W., & Shi, Y. (2001) · Science · doi:10.1126/science.1062236 · Cited by 177

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 167

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 165

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

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 151

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 61

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

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

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

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

Ubiquitin biology: an old dog learns an old trick

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

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

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

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

Derynck, R., & Zhang, Y. E. (2003) · Nature · doi:10.1038/nature02006 · Cited by 5,498

Cell Death

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

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 3,370

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

Inhibitors of Apoptosis Proteins in Injury and Disease

Lotocki, G., & Keane, R. W. (2002) · IUBMB Life · doi:10.1080/15216540215675 · Cited by 24

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

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

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

Advances in studies on inhibitor of apoptosis proteins

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