Cited by 1,756Cell death mechanisms and regulationCancer-related Molecular PathwaysUbiquitin and proteasome pathways

The DOI matches its Crossref record; 158 of the 158 references it cites were found in a registry or an index.

IAP proteins: blocking the road to death's door

Salvesen, Guy S., Duckett, Colin S.·2002·Nature Reviews Molecular Cell Biology

Open this paper in CoChat — free account

Abstract

The 'inhibitor of apoptosis' (IAP) gene family, which was discovered less than a decade ago, encodes a group of structurally related proteins that, in addition to their ability to suppress apoptotic cell death, are involved in an increasing number of seemingly unrelated cellular functions. Here, we review the functional and structural properties of this fascinating group of proteins, and of several recently identified IAP-binding factors that regulate IAP function.

Integrity signals

Registry

Crossref · 10.1038/nrm830

Cites

158 of 158 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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

Show all 157 references

Sorted by citations

Items 201–300 of 1,000

Targeting the Fas/FasL signaling pathway in cancer therapy
Villa‐Morales, M., & Fernández‐Piqueras, J. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.628937 · Cited by 155
MicroRNAs as therapeutic targets in chemoresistance
Garofalo, M., & Croce, C. M. (2013) · Drug Resistance Updates · doi:10.1016/j.drup.2013.05.001 · Cited by 156
The Apical Caspase dronc Governs Programmed and Unprogrammed Cell Death in Drosophila
Chew, S. K., Akdemir, F., Chen, P., Lu, W.-J., Mills, K., Daish, T., Kumar, S., Rodriguez, A., & Abrams, J. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.09.016 · Cited by 153
Requirement of Both the Second and Third BIR Domains for the Relief of X-linked Inhibitor of Apoptosis Protein (XIAP)-mediated Caspase Inhibition by Smac
Huang, Y., Rich, R. L., Myszka, D. G., & Wu, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310061200 · Cited by 152
Inhibitors of Apoptotic Proteins: New Targets for Anticancer Therapy
Saleem, M., Qadir, M. I., Perveen, N., Ahmad, B., Saleem, U., Irshad, T., & Ahmad, B. (2013) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12176 · Cited by 151
Programmed Cell Death Pathways and Current Antitumor Targets
Tan, M., Ooi, J. P., Ismail, N. I., Moad, A. I. H., & Muhammad, T. S. T. (2009) · Pharmaceutical Research · doi:10.1007/s11095-009-9895-1 · Cited by 156
Dying a Thousand Deaths: Redundant Pathways From Different Organelles to Apoptosis and Necrosis
Lemasters, J. J. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.06.006 · Cited by 154
Emerging Role of Protein-Protein Transnitrosylation in Cell Signaling Pathways
Nakamura, T., & Lipton, S. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4703 · Cited by 151
Survivin Modulates Microtubule Dynamics and Nucleation throughout the Cell Cycle
Rosa, J., Canovas, P. M., Islam, A., Altieri, D. C., & Doxsey, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0723 · Cited by 150
Small Molecule XIAP Inhibitors Enhance TRAIL-Induced Apoptosis and Antitumor Activity in Preclinical Models of Pancreatic Carcinoma
Vogler, M., Walczak, H., Stadel, D., Haas, T. L., Genze, F., Jovanovic, M., Bhanot, U. K., Hasel, C., Möller, P., Gschwend, J. E., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2436 · Cited by 151
Anti-apoptotic effect of granulocyte-colony stimulating factor after focal cerebral ischemia in the rat
Solaroğlu, İ., Tsubokawa, T., Cahill, J., & Zhang, J. H. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.09.014 · Cited by 149
Critical function of endogenous XIAP in regulating caspase activation during sympathetic neuronal apoptosis
Potts, P. R., Singh, S., Knezek, M., Thompson, C. B., & Deshmukh, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200307130 · Cited by 149
Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination
Chai, J., Yan, N., Huh, J. R., Wu, J., Li, W., Hay, B. A., & Shi, Y. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb989 · Cited by 149
Targeting caspases in cancer therapeutics
Hensley, P. J., Mishra, M., & Kyprianou, N. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0128 · Cited by 148
Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5
Adams, C., Totpal, K., Lawrence, D., Marsters, S., Pitti, R., Yee, S., Ross, S., Deforge, L., Koeppen, H., Sagolla, M., et al. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402306 · Cited by 148
Targeting XIAP Bypasses Bcl-2–Mediated Resistance to TRAIL and Cooperates with TRAIL to Suppress Pancreatic Cancer Growth In vitro and In vivo
Vogler, M., Walczak, H., Stadel, D., Haas, T. L., Genze, F., Jovanovic, M., Gschwend, J. E., Simmet, T., Debatin, K., & Fulda, S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1296 · Cited by 149
PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis
Saita, S., Nolte, H., Fiedler, K. U., Kashkar, H., Venne, A. S., Zahedi, R. P., Krüger, M., & Langer, T. (2017) · Nature Cell Biology · doi:10.1038/ncb3488 · Cited by 152
Protein synthesis in eukaryotes: The growing biological relevance of cap-independent translation initiation
López‐Lastra, M., RIVAS, A., & Barría, M. I. (2005) · Biological Research · doi:10.4067/s0716-97602005000200003 · Cited by 158
The Role of Apoptosis in Defense Against Baculovirus Infection in Insects
Clem, R. J. (2005) · Springer eBooks · doi:10.1007/3-540-27320-4_5 · Cited by 146
Survivin As a Therapeutic Target for Radiation Sensitization in Lung Cancer
Lü, B., Mu, Y. M., Cao, C., Zeng, F., Schneider‐Burrus, S., Tan, J., Price, J., Chen, J., Freeman, M. L., & Hallahan, D. E. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3547 · Cited by 145
Apoptosis in cancer—implications for therapy
Schulze‐Bergkamen, H., & Krammer, P. H. (2004) · Seminars in Oncology · doi:10.1053/j.seminoncol.2003.11.006 · Cited by 146
A small molecule Smac-mimic compound induces apoptosis and sensitizes TRAIL- and etoposide-induced apoptosis in breast cancer cells
Bockbrader, K., Tan, M., & Sun, Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208888 · Cited by 144
Design, synthesis and biological evaluation of nuclear receptor-degradation inducers
Itoh, Y., Kitaguchi, R., Ishikawa, M., Naito, M., & Hashimoto, Y. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.041 · Cited by 143
Axonal Degeneration Is Regulated by the Apoptotic Machinery or a NAD + -Sensitive Pathway in Insects and Mammals
Schoenmann, Z., Assa-Kunik, E., Tiomny, S., Minis, A., Haklai-Topper, L., Arama, E., & Yaron, A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0922-10.2010 · Cited by 147
Survivin and apoptosis control
Altieri, D. C. (2003) · Advances in cancer research · doi:10.1016/s0065-230x(03)88303-3 · Cited by 142
Acute Ablation of Survivin Uncovers p53-dependent Mitotic Checkpoint Functions and Control of Mitochondrial Apoptosis
Beltrami, E., Plescia, J., Wilkinson, J. C., Duckett, C. S., & Altieri, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309479200 · Cited by 142
Self-citation
Covalent Inhibitors of Protein–Protein Interactions Targeting Lysine, Tyrosine, or Histidine Residues
Gambini, L., Baggio, C., Udompholkul, P., Jossart, J. N., Salem, A. F., Perry, J. J. P., & Pellecchia, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00561 · Cited by 143
Future Therapeutic Directions for Smac-Mimetics
Morrish, E., Brumatti, G., & Silke, J. (2020) · Cells · doi:10.3390/cells9020406 · Cited by 151
Lysosomal cysteine cathepsins: signaling pathways in apoptosis
Stoka, V., Türk, V., & Turk, B. (2007) · Biological Chemistry · doi:10.1515/bc.2007.064 · Cited by 141
Targeting Apoptosis with Dietary Bioactive Agents
Martin, K. R. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100201 · Cited by 140
The Apaf‐1•procaspase‐9 apoptosome complex functions as a proteolytic‐based molecular timer
Malladi, S., Challa-Malladi, M., Fearnhead, H. O., & Bratton, S. B. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.152 · Cited by 140
Translational Induction of the Inhibitor of Apoptosis Protein HIAP2 during Endoplasmic Reticulum Stress Attenuates Cell Death and Is Mediated via an Inducible Internal Ribosome Entry Site Element
Warnakulasuriyarachchi, D., Cerquozzi, S., Cheung, H. H., & Holčı́k, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308737200 · Cited by 139
The dependence receptor hypothesis
Mehlen, P., & Bredesen, D. E. (2004) · APOPTOSIS · doi:10.1023/b:appt.0000012120.66221.b2 · Cited by 138
Small molecule XIAP inhibitors cooperate with TRAIL to induce apoptosis in childhood acute leukemia cells and overcome Bcl-2–mediated resistance
Fakler, M., Loeder, S., Vogler, M., Schneider, K., Jeremias, I., Debatin, K., & Fulda, S. (2008) · Blood · doi:10.1182/blood-2007-09-114314 · Cited by 138
Resistance to chemotherapy and hormone therapy in endometrial cancer
Chaudhry, P., & Asselin, É. (2009) · Endocrine Related Cancer · doi:10.1677/erc-08-0266 · Cited by 137
Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP
Vucic, D., Franklin, M. C., Wallweber, H. J. A., Kanad, D. A. S., Eckelman, B. P., Shin, H., Elliott, L. O., Kadkhodayan, S., Deshayes, K., Salvesen, G. S., et al. (2004) · Biochemical Journal · doi:10.1042/bj20041108 · Cited by 136
Self-citation
Effects of Bcl-2 Levels on Fas Signaling-Induced Caspase-3 Activation: Molecular Genetic Tests of Computational Model Predictions
Hua, F., Cornejo, M., Cardone, M. H., Stokes, C. L., & Lauffenburger, D. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.2.985 · Cited by 136
XIAP inhibits autophagy via XIAP‐Mdm2‐p53 signalling
Huang, X., Wu, Z., Mei, Y., & Wu, M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.133 · Cited by 138
Glutamine metabolism in breast cancer and possible therapeutic targets
Li, S., Zeng, H., Fan, J., Wang, X., Xu, C., Li, Y., Tu, J., Nephew, K. P., & Long, X. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115464 · Cited by 143
Bax and Bak Are Required for Apoptosis Induction by Sulforaphane, a Cruciferous Vegetable–Derived Cancer Chemopreventive Agent
Choi, S., & Singh, S. V. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3616 · Cited by 135
A Ubiquitin Ligase Complex Regulates Caspase Activation During Sperm Differentiation in Drosophila
Arama, E., Bader, M., Rieckhof, G. E., & Steller, H. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050251 · Cited by 136
Plant programmed cell death: can't live with it; can't live without it
Williams, B., & Dickman, M. (2008) · Molecular Plant Pathology · doi:10.1111/j.1364-3703.2008.00473.x · Cited by 134
Long non-coding RNA ANRIL is up-regulated in bladder cancer and regulates bladder cancer cell proliferation and apoptosis through the intrinsic pathway
Zhu, H., Li, X., Song, Y., Zhang, P., Xiao, Y., & Xing, Y. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.002 · Cited by 133
The neem limonoids azadirachtin and nimbolide induce cell cycle arrest and mitochondria-mediated apoptosis in human cervical cancer (HeLa) cells
Priyadarsini, R. V., Murugan, R. S., Sripriya, P., Karunagaran, D., & Nagini, S. (2010) · Free Radical Research · doi:10.3109/10715761003692503 · Cited by 132
Ischemic Preconditioning: Neuronal Survival in the Face of Caspase-3 Activation
Tanaka, H., Yokota, H., Jover, T., Cappuccio, I., Calderone, A., Simionescu, M., Bennett, M. V. L., & Zukin, R. S. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5475-03.2004 · Cited by 131
Anti-apoptotic signalling by the Dot/Icm secretion system ofL. pneumophila
Abu-Zant, A., Jones, S. C., Asare, R., Suttles, J., Price, C. T. D., Graham, J. E., & Kwaik, Y. A. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00785.x · Cited by 145
Structure-Based Design, Synthesis, and Evaluation of Conformationally Constrained Mimetics of the Second Mitochondria-Derived Activator of Caspase That Target the X-Linked Inhibitor of Apoptosis Protein/Caspase-9 Interaction Site
Sun, H., Nikolovska‐Coleska, Z., Yang, C., Xu, L., Tomita, Y. A., Krajewski, K., Roller, P. P., & Wang, S. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0499108 · Cited by 133
Silver nanoparticles of Albizia adianthifolia: the induction of apoptosis in human lung carcinoma cell line
Govender, R., Phulukdaree, A., Gengan, R. M., Anand, K., & Chuturgoon, A. A. (2013) · Journal of Nanobiotechnology · doi:10.1186/1477-3155-11-5 · Cited by 133
Regulation of death receptor signaling by the ubiquitin system
Wertz, I. E., & Dixit, V. M. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.168 · Cited by 134
Proteinaceous cysteine protease inhibitors
Dubin, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4445-9 · Cited by 129
Inhibition of caspase activation and a requirement for NF-κB function in theToxoplasma gondii-mediated blockade of host apoptosis
Payne, T. M., Molestina, R. E., & Sinai, A. P. (2003) · Journal of Cell Science · doi:10.1242/jcs.00756 · Cited by 128
IAP Family of Cell Death and Signaling Regulators
Silke, J., & Vucic, D. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801430-1.00002-0 · Cited by 138
Caspases, apoptosis and aging
Zhang, J., Zhang, Y., & Herman, B. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00026-6 · Cited by 129
Genetic control of programmed cell death (apoptosis) in Drosophila
Xu, D., Woodfield, S. E., Lee, T. V., Fan, Y., Antonio, C., & Bergmann, A. (2009) · Fly · doi:10.4161/fly.3.1.7800 · Cited by 132
Molecular circuits of apoptosis regulation and cell division control: The survivin paradigm
Altieri, D. C. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20140 · Cited by 127
Caspases and apoptosis in fish
Takle, H., & Andersen, Ø. (2007) · Journal of Fish Biology · doi:10.1111/j.1095-8649.2007.01665.x · Cited by 132
IAPs regulate the plasticity of cell migration by directly targeting Rac1 for degradation
Oberoi‐Khanuja, T. K., Dogan, T., Hocking, J. C., Scholz, R., Mooz, J., Anderson, C. L., Karreman, C., zu Heringdorf, D. M., Schmidt, G., Ruonala, M. O., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.423 · Cited by 125
Translational and posttranslational regulation of XIAP by eIF2α and ATF4 promotes ER stress–induced cell death during the unfolded protein response
Hiramatsu, N., Messah, C., Han, J., LaVail, M. M., Kaufman, R. J., & Lin, J. H. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0664 · Cited by 135
Comparative Proteomics of Colon Cancer Stem Cells and Differentiated Tumor Cells Identifies BIRC6 as a Potential Therapeutic Target
van Houdt, W. J., Emmink, B. L., Pham, T., Piersma, S. R., Verheem, A., Vries, R. J. L. D., Fratantoni, S., Pronk, A., Clevers, H. C., Rinkes, I. H. M. B., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.011353 · Cited by 125
Into the heart: The emerging role of the ubiquitin–proteasome system
Willis, M. S., & Patterson, C. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.07.015 · Cited by 125
Nrdp1‐mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis
Qiu, X., Markant, S. L., Yuan, J., & Goldberg, A. L. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600075 · Cited by 125
Anti-inflammatory, pro-apoptotic, and anti-proliferative effects of a methanolic neem (Azadirachta indica) leaf extract are mediated via modulation of the nuclear factor-κB pathway
Schumacher, M. M., Cerella, C., Reuter, S., Dicato, M. A., & Diederich, M. F. (2010) · Genes & Nutrition · doi:10.1007/s12263-010-0194-6 · Cited by 124
Carotenoids in Cancer Apoptosis—The Road from Bench to Bedside and Back
Koklesová, L., Líšková, A., Samec, M., Buhrmann, C., Samuel, S. M., Varghese, E., Ashrafizadeh, M., Najafi, M., Shakibaei, M., Büsselberg, D., et al. (2020) · Cancers · doi:10.3390/cancers12092425 · Cited by 128
The insect caspases
Cooper, D., Granville, D. J., & Lowenberger, C. A. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0322-1 · Cited by 123
Essential Role for Survivin in Early Brain Development
Jiang, Y., de Bruin, A., Caldas, H., Fangusaro, J., Hayes, J., Conway, E. M., Robinson, M. L., & Altura, R. A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1446-05.2005 · Cited by 123
Fisetin, a natural flavonoid, targets chemoresistant human pancreatic cancer AsPC‐1 cells through DR3‐mediated inhibition of NF‐κB
Murtaza, I., Adhami, V. M., Hafeez, B. B., Saleem, M., & Mukhtar, H. (2009) · International Journal of Cancer · doi:10.1002/ijc.24628 · Cited by 122
Development and Characterization of Nonpeptidic Small Molecule Inhibitors of the XIAP/Caspase-3 Interaction
Wu, T. Y.-H., Wagner, K. W., Bursulaya, B. D., Schultz, P. G., & Deveraux, Q. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00157-1 · Cited by 122
β-Catenin Overexpression Reduces Myocardial Infarct Size through Differential Effects on Cardiomyocytes and Cardiac Fibroblasts
Hahn, J., Cho, H.-J., Bae, J.-W., Yuk, H.-S., Kim, K., Park, K. W., Koo, B.-K., Chae, I., Shin, C.-S., Oh, B., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603916200 · Cited by 124
Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2
Blankenship, J. W., Varfolomeev, E. E., Goncharov, T., Fedorova, A. V., Kirkpatrick, D. S., Izrael-Tomasevic, A., Phu, L., Arnott, D. P., Aghajan, M., Zobel, K., et al. (2008) · Biochemical Journal · doi:10.1042/bj20081885 · Cited by 122
Selective CDK9 inhibition overcomes TRAIL resistance by concomitant suppression of cFlip and Mcl-1
Lemke, J., von Karstedt, S., Hay, M. Y. A. E., Conti, A., Vargas, F. A., Montinaro, A., Papenfuss, K., El-Bahrawy, M. A., & Walczak, H. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.179 · Cited by 123
Topoisomerase degradation, DSB repair, p53 and IAPs in cancer cell resistance to camptothecin-like topoisomerase I inhibitors
Tomicic, M. T., & Kaina, B. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.09.002 · Cited by 123
Gene-expression profiling identifies distinct subclasses of core binding factor acute myeloid leukemia
Bullinger, L., Rücker, F. G., Kurz, S., Du, J., Scholl, C., Sander, S., Corbacioglu, A., Lottaz, C., Krauter, J., Fröhling, S., et al. (2007) · Blood · doi:10.1182/blood-2006-10-049783 · Cited by 122
Nuclear export is essential for the tumor‐promoting activity of survivin
Knauer, S. K., Krämer, O. H., Knösel, T., Engels, K., Rödel, F., Kovács, A. F., Dietmaier, W., Klein‐Hitpaß, L., Habtemichael, N., Schweitzer, A., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-5741com · Cited by 121
Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth
McDonald, E. R., & El‐Deiry, W. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307459101 · Cited by 121
Pro-apoptotic Proteins Released from the Mitochondria Regulate the Protein Composition and Caspase-processing Activity of the Native Apaf-1/Caspase-9 Apoptosome Complex
Twiddy, D., Brown, D. G., Adrain, C., Jukes, R., Martin, S. J., Cohen, G. M., MacFarlane, M., & Cain, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311388200 · Cited by 119
Kunitz Trypsin Inhibitor: An Antagonist of Cell Death Triggered by Phytopathogens and Fumonisin B1 in Arabidopsis
Li, J., Brader, G., & Palva, E. T. (2008) · Molecular Plant · doi:10.1093/mp/ssn013 · Cited by 119
Discovery of a Novel Class of Dimeric Smac Mimetics as Potent IAP Antagonists Resulting in a Clinical Candidate for the Treatment of Cancer (AZD5582)
Hennessy, E. J., Adam, A., Aquila, B. M., Castriotta, L., Cook, D. J., Hattersley, M. M., Hird, A. W., Huntington, C., Kamhi, V. M., Laing, N. M., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401075x · Cited by 119
Sulfur alleviates arsenic toxicity by reducing its accumulation and modulating proteome, amino acids and thiol metabolism in rice leaves
Awasthi, G., Singh, A. P., Kumar, A., Dwivedi, S. K., Deeba, F., Kumar, S., Suman, S., Adhikari, B., Shukla, Y., Trivedi, P. K., et al. (2015) · Scientific Reports · doi:10.1038/srep16205 · Cited by 118
Protein quality control and degradation in cardiomyocytes
Wang, X., Su, H., & Ranek, M. J. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.03.025 · Cited by 120
Targeting XIAP for Promoting Cancer Cell Death—The Story of ARTS and SMAC
Abbas, R., & Larisch, S. (2020) · Cells · doi:10.3390/cells9030663 · Cited by 125
Chemotherapy Resistance Explained through Endoplasmic Reticulum Stress-Dependent Signaling
Bahar, E., Kim, J., & Yoon, H. (2019) · Cancers · doi:10.3390/cancers11030338 · Cited by 117
Reduced Apaf-1 levels in cardiomyocytes engage strict regulation of apoptosis by endogenous XIAP
Potts, M. B., Vaughn, A. E., McDonough, H., Patterson, C., & Deshmukh, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504082 · Cited by 116
Natural products: a hope for glioblastoma patients
Vengoji, R., Macha, M. A., Batra, S. K., & Shonka, N. (2018) · Oncotarget · doi:10.18632/oncotarget.25175 · Cited by 117
Post-Translational Modifications in NETosis and NETs-Mediated Diseases
Hamam, H. J., & Palaniyar, N. (2019) · Biomolecules · doi:10.3390/biom9080369 · Cited by 119
Antitumor Activity of Capsaicin on Human Colon Cancer Cells in Vitro and Colo 205 Tumor Xenografts in Vivo
Lu, H.-F., Chen, Y.-L., Yang, J., Yang, Y., Liu, J.-Y., Hsu, S., Lai, K., & Chung, J. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103335w · Cited by 115
Acute neuroprotective synergy of erythropoietin and insulin-like growth factor I
Digicaylioglu, M. H., Garden, G. A., Timberlake, S. C., Fletcher, L., & Lipton, S. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403172101 · Cited by 115
Targeting Apoptotic Pathways in Cancer Cells
Denicourt, C., & Dowdy, S. F. (2004) · Science · doi:10.1126/science.1102974 · Cited by 114
Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function
Wright, C. W. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26251 · Cited by 114
Redox regulation of protein misfolding, mitochondrial dysfunction, synaptic damage, and cell death in neurodegenerative diseases
Nakamura, T., Cho, D., & Lipton, S. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.032 · Cited by 114
Inhibitor of Apoptosis Protein (IAP) Antagonists in Anticancer Agent Discovery: Current Status and Perspectives
Cong, H., Xu, L., Wu, Y., Qu, Z., Bian, T., Zhang, W., Xing, C., & Zhuang, C. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01668 · Cited by 119
Netrin-1: when a neuronal guidance cue turns out to be a regulator of tumorigenesis
Mehlen, P., & Furne, C. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5191-3 · Cited by 119
Caspase-mediated cleavage converts Livin from an antiapoptotic to a proapoptotic factor: implications for drug-resistant melanoma.
Nachmias, B., Ashhab, Y., Bucholtz, V., Drize, O., Kadouri, L., Lotem, M., Tamar, P., Mandelboim, O., & Ben‐Yehuda, D. (2003) · PubMed · Cited by 113
IAPs: Guardians of RIPK1
Darding, M., & Meier, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.163 · Cited by 118
cIAP1 Localizes to the Nuclear Compartment and Modulates the Cell Cycle
Samuel, T., Okada, K., Hyer, M. L., Welsh, K., Zapata, J. M., & Reed, J. C. (2005) · Cancer Research · doi:10.1158/0008-5472.210.65.1 · Cited by 112
Bcl-2 Family Members as Sentinels of Cellular Integrity and Role of Mitochondrial Intermembrane Space Proteins in Apoptotic Cell Death
Festjens, N., van Gurp, M., Loo, G., Saelens, X., & Vandenabeele, P. (2003) · Acta Haematologica · doi:10.1159/000074483 · Cited by 115
Mcl-1 Is a Key Regulator of Apoptosis Resistance in Chlamydia trachomatis-Infected Cells
Rajalingam, K., Sharma, M., Lohmann, C., Oswald, M., Thieck, O., Froelich, C. J., & Rudel, T. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003102 · Cited by 112
Gene discovery, comparative analysis and expression profile reveal the complexity of the Crassostrea gigas apoptosis system
Zhang, L., Li, L., & Zhang, G. (2011) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2011.01.005 · Cited by 111
Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim
Yan, N., Wu, J.-W., Chai, J., Li, W., & Shi, Y. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb764 · Cited by 111
E2F1 Overexpression Correlates with Thymidylate Synthase and Survivin Gene Expressions and Tumor Proliferation in Non–Small-Cell Lung Cancer
Huang, C., Liu, D., Nakano, J., Yokomise, H., Ueno, M., Kadota, K., & Wada, H. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1539 · Cited by 111
MAPKs: new targets for neurodegeneration
Harper, S. J., & Wilkie, N. M. (2003) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.7.2.187 · Cited by 111

Authors: Salvesen, G. S., & Duckett, C. S.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
University of Michigan (US)
Corresponding author: Duckett, Colin S.
ORCID: Salvesen, Guy S.
Duckett, Colin S.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2002-06
Volume: 3
Issue: 6
Pages: 401-410
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm830
OpenAlex: W1492587973
Semantic Scholar: 37eaa4d6440b014eff358aeee58f3772e77e8934
Cited by: 1,756
References: 157
Citations by year: 2026: 12 · 2025: 8 · 2024: 20 · 2023: 25 · 2022: 26 · 2021: 32 · 2020: 46 · 2019: 48 · 2018: 42 · 2017: 43 · 2016: 43 · 2015: 59 · 2014: 63 · 2013: 90 · 2012: 81
FWCI: 9.92
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: inhibitor of apoptosis proteins, apoptosis, cell death regulation, protein structure
MeSH terms: Animals, Binding Sites, Gene Expression Regulation, Humans, Proteins, Cysteine Proteinase Inhibitors, Apoptosis, Insect Proteins, Inhibitor of Apoptosis Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

IAP proteins: blocking the road to death's door

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks