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

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

Clonogenic assay of cells in vitro

Franken, N. A. P., Rodermond, H. M., Stap, J., HAVEMAN, J., & Chris van, B. R. E. E. (2006) · Nature Protocols · doi:10.1038/nprot.2006.339 · Cited by 4,202 · see citing works

Signaling to NF-κB

Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842 · 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

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

Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738 · 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

Mechanisms and Genes of Cellular Suicide

Steller, H. (1995) · Science · doi:10.1126/science.7878463 · Cited by 2,465 · 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

TNF-R1 Signaling: A Beautiful Pathway

Chen, G., & Goeddel, D. V. (2002) · Science · doi:10.1126/science.1071924 · Cited by 1,930 · see citing works

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling

Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,852 · see citing works

IAP proteins: blocking the road to death's door

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

Activation by IKKα of a Second, Evolutionary Conserved, NF-κB Signaling Pathway

Senftleben, U., Cao, Y., Xiao, G., Greten, F. R., Krähn, G. M., Bonizzi, G., Chen, Y., Hu, Y., Fong, A., Sun, S., et al. (2001) · Science · doi:10.1126/science.1062677 · Cited by 1,361 · see citing works

Apoptosis control by death and decoy receptors

Ashkenazi, A., & Dixit, V. M. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80034-9 · Cited by 1,281 · see citing works

Ubiquitin signalling in the NF-κB pathway

Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184 · 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

A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor

Rothe, M., Wong, S. C., Henzel, W. J., & Goeddel, D. V. (1994) · Cell · doi:10.1016/0092-8674(94)90532-0 · Cited by 1,054 · 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

Promiscuous Mutations Activate the Noncanonical NF-κB Pathway in Multiple Myeloma

Keats, J. J., Fonseca, R., Chesi, M., Schop, R., Baker, A., Chng, W.-J., Van Wier, S., Tiedemann, R., Shi, C.-X., Sebag, M., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.07.003 · Cited by 983 · 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

Frequent Engagement of the Classical and Alternative NF-κB Pathways by Diverse Genetic Abnormalities in Multiple Myeloma

Annunziata, C. M., Davis, R. E., Demchenko, Y., Bellamy, W., Gabrea, A., Zhan, F., Lenz, G., Hanamura, I., Wright, G., Xiao, W., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.07.004 · Cited by 952 · 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

NF-κB-Inducing Kinase Regulates the Processing of NF-κB2 p100

Xiao, G., Harhaj, E. W., & Sun, S. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00187-3 · Cited by 836 · see citing works

IκB kinase complexes: gateways to NF-κB activation and transcription

Scheidereit, C. (2006) · Oncogene · doi:10.1038/sj.onc.1209934 · Cited by 652 · 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

A Small Molecule Smac Mimic Potentiates TRAIL- and TNFα-Mediated Cell Death

Li, L., Thomas, R., Suzuki, H., Brabander, J. D., Wang, X.-D., & Harran, P. G. (2004) · Science · doi:10.1126/science.1098231 · Cited by 620 · 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

The inhibitors of apoptosis (IAPs) as cancer targets

Hunter, A. M., LaCasse, E. C., & Korneluk, R. G. (2007) · Apoptosis · doi:10.1007/s10495-007-0087-3 · Cited by 565 · see citing works

The CARD domain: a new apoptotic signalling motif

Hofmann, K. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01043-8 · Cited by 537 · see citing works

Apoptosis-targeted therapies for cancer

Reed, J. C. (2003) · Cancer Cell · doi:10.1016/s1535-6108(02)00241-6 · Cited by 502 · 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

The inhibitors of apoptosis: there is more to life than Bcl2

Liston, P., Fong, W. G., & Korneluk, R. G. (2003) · Oncogene · doi:10.1038/sj.onc.1207101 · Cited by 440 · see citing works

The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex

Shu, H., Takeuchi, M., & Goeddel, D. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13973 · Cited by 418 · 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

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

Discovery of Potent Antagonists of the Antiapoptotic Protein XIAP for the Treatment of Cancer

Oost, T. K., Sun, C. C., Armstrong, R. C., Al-Assaad, A.-S., Betz, S. F., Deckwerth, T. L., Ding, H., Elmore, S. W., Meadows, R. P., Olejniczak, E. T., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040037k · Cited by 367 · see citing works

Molecular Determinants of Kinase Pathway Activation by Apo2 Ligand/Tumor Necrosis Factor-related Apoptosis-inducing Ligand

Varfolomeev, E. E., Maecker, H. L., Sharp, D. A., Lawrence, D. A., Renz, M. E., Vucic, D., & Ashkenazi, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509560200 · Cited by 278 · see citing works

Alterations in the apoptotic machinery and their potential role in anticancer drug resistance

Kaufmann, S. H., & Vaux, D. L. (2003) · Oncogene · doi:10.1038/sj.onc.1206945 · Cited by 265 · see citing works

Caspase activation – stepping on the gas or releasing the brakes? Lessons from humans and flies

Salvesen, G. S., & Abrams, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207522 · Cited by 237 · see citing works

TRAF2 Differentially Regulates the Canonical and Noncanonical Pathways of NF-κB Activation in Mature B Cells

Grech, A. P., Amesbury, M., Chan, T. D., Gardam, S., Basten, A., & Brink, R. A. (2004) · Immunity · doi:10.1016/j.immuni.2004.09.011 · Cited by 216 · see citing works

Smac/DIABLO Selectively Reduces the Levels of c-IAP1 and c-IAP2 but Not That of XIAP and Livin in HeLa Cells

Yang, Q.-H., & Du, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401253200 · Cited by 213 · see citing works

Design, Synthesis, and Biological Activity of a Potent Smac Mimetic That Sensitizes Cancer Cells to Apoptosis by Antagonizing IAPs

Zobel, K., Wang, L., Varfolomeev, E. E., Franklin, M. C., Elliott, L. O., Wallweber, H. J. A., Okawa, D. C., Flygare, J. A., Vucic, D., Fairbrother, W. J., et al. (2006) · ACS Chemical Biology · doi:10.1021/cb600276q · Cited by 175 · see citing works

Distinct BIR Domains of cIAP1 Mediate Binding to and Ubiquitination of Tumor Necrosis Factor Receptor-associated Factor 2 and Second Mitochondrial Activator of Caspases

Samuel, T., Welsh, K., Lober, T., Togo, S. H., Zapata, J. M., & Reed, J. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509381200 · Cited by 171 · 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

Structure-Based Design of Potent, Conformationally Constrained Smac Mimetics

Sun, H., Nikolovska‐Coleska, Z., Yang, C., Xu, L., Liu, M., Tomita, Y. A., Pan, H., Yoshioka, Y., Krajewski, K., Roller, P. P., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047438+ · Cited by 159 · see citing works

Selective Knockdown of the Long Variant of Cellular FLICE Inhibitory Protein Augments Death Receptor-mediated Caspase-8 Activation and Apoptosis

Sharp, D. A., Lawrence, D. A., & Ashkenazi, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413962200 · Cited by 152 · see citing works

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 · see citing works

A Dimeric Smac/Diablo Peptide Directly Relieves Caspase-3 Inhibition by XIAP

Gao, Z., Tian, Y., Wang, J., Yin, Q., Wu, H., Li, Y. M., & Jiang, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705258200 · Cited by 108 · see citing works

The Inhibitor of Apoptosis Protein Fusion c-IAP2·MALT1 Stimulates NF-κB Activation Independently of TRAF1 AND TRAF2

Varfolomeev, E. E., Wayson, S. M., Dixit, V. M., Fairbrother, W. J., & Vucic, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605116200 · Cited by 89 · see citing works

Development of Peptidomimetics Targeting IAPs

SHARMA, S. K., Straub, C. S., & Zawel, L. S. (2006) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-005-9003-2 · Cited by 61 · see citing works

[57] Dye uptake method for assay of interferon activity

Johnston, M., Finter, N. B., & Young, P. A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(81)78147-3 · Cited by 35 · see citing works

Shared Principles in NF-κB Signaling

Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,814 · see citing works

Mitochondria and cell death: outer membrane permeabilization and beyond

Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · see citing works

Regulation and Function of NF-κB Transcription Factors in the Immune System

Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,578 · see citing works

Mitochondria as multifaceted regulators of cell death

Bock, F. J., & Tait, S. W. G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0173-8 · Cited by 2,482 · see citing works

Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α

He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214 · see citing works

Necroptosis and its role in inflammation

Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148 · see citing works

NF-κB in biology and targeted therapy: new insights and translational implications

Guo, Q., Jin, Y., Chen, X., Ye, X., Shen, X., Lin, M., Zeng, C., Zhou, T., & Zhang, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01757-9 · Cited by 2,267 · see citing works

The non-canonical NF-κB pathway in immunity and inflammation

Sun, S. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.52 · Cited by 1,911 · see citing works

Regulated necrosis: the expanding network of non-apoptotic cell death pathways

Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works

NF-κB, the first quarter-century: remarkable progress and outstanding questions

Hayden, M. S., & Ghosh, S. (2012) · Genes & Development · doi:10.1101/gad.183434.111 · Cited by 1,693 · see citing works

Ubiquitination in disease pathogenesis and treatment

Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,405 · see citing works

TNF-α Induces Two Distinct Caspase-8 Activation Pathways

Wang, L., Du, F., & Wang, X. (2008) · Cell · doi:10.1016/j.cell.2008.03.036 · Cited by 1,352 · see citing works

Non-canonical NF-κB signaling pathway

Sun, S. (2010) · Cell Research · doi:10.1038/cr.2010.177 · Cited by 1,200 · see citing works

Regulation of NF-κB by TNF family cytokines

Hayden, M. S., & Ghosh, S. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.05.004 · Cited by 1,116 · 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

Is NF-κB a good target for cancer therapy? Hopes and pitfalls

Baud, V., & Karin, M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2781 · Cited by 1,059 · see citing works

Regulation of tumour necrosis factor signalling: live or let die

Brenner, D., Blaser, H., & Mak, T. W. (2015) · Nature Reviews Immunology · doi:10.1038/nri3834 · Cited by 998 · see citing works

Mitochondrial control of inflammation

Marchi, S., Guilbaud, E., Tait, S. W. G., Yamazaki, T., & Galluzzi, L. (2023) · Nature Reviews Immunology · doi:10.1038/s41577-022-00760-x · Cited by 1,027 · see citing works

The many roles of FAS receptor signaling in the immune system

Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968 · see citing works

cIAPs Block Ripoptosome Formation, a RIP1/Caspase-8 Containing Intracellular Cell Death Complex Differentially Regulated by cFLIP Isoforms

Feoktistova, M., Geserick, P., Kellert, B., Panayotova‐Dimitrova, D., Langlais, C., Hupe, M., Cain, K., MacFarlane, M., Häcker, G. A., & Leverkus, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.011 · Cited by 855 · 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

The TRAIL apoptotic pathway in cancer onset, progression and therapy

Johnstone, R. W., Frew, A. J., & Smyth, M. J. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2465 · Cited by 835 · see citing works

PROteolysis TArgeting Chimeras (PROTACs) — Past, present and future

Pettersson, M., & Crews, C. M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.01.002 · Cited by 818 · see citing works

The Ripoptosome, a Signaling Platform that Assembles in Response to Genotoxic Stress and Loss of IAPs

Tenev, T., Bianchi, K., Darding, M., Broemer, M., Langlais, C., Wållberg, F., Zachariou, A., Lopez, J. S., MacFarlane, M., Cain, K., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.006 · Cited by 818 · see citing works

IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer

Gyrd-Hansen, M., & Meier, P. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2889 · Cited by 790 · see citing works

The noncanonical NF‐κB pathway

Sun, S. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01088.x · Cited by 724 · see citing works

Life and death by death receptors

Guicciardi, M. E., & Gores, G. J. (2009) · The FASEB Journal · doi:10.1096/fj.08-111005 · Cited by 689 · see citing works

Tumor necrosis factor and cancer, buddies or foes?

Wang, X., & Lin, Y. (2008) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2008.00889.x · Cited by 730 · see citing works

Ubiquitylation in innate and adaptive immunity

Bhoj, V. G., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature07959 · Cited by 632 · see citing works

Regulated necrosis: disease relevance and therapeutic opportunities

Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works

Live to die another way: modes of programmed cell death and the signals emanating from dying cells

Fuchs, Y., & Steller, H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3999 · Cited by 632 · see citing works

Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling

Vallabhapurapu, S., Matsuzawa, A., Zhang, W., Tseng, P., Keats, J. J., Wang, H., Vignali, D. A. A., Bergsagel, P. L., & Karin, M. (2008) · Nature Immunology · doi:10.1038/ni.1678 · Cited by 605 · see citing works

Noncanonical NF-κB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK

Zarnegar, B. J., Wang, Y., Mahoney, D. J., Dempsey, P. W., Cheung, H. H., He, J., Shiba, T. L., Yang, X., Yeh, W., Mak, T. W., et al. (2008) · Nature Immunology · doi:10.1038/ni.1676 · Cited by 607 · see citing works

Molecular Mechanisms of Apoptosis and Roles in Cancer Development and Treatment

Goldar, S., Khaniani, M. S., Derakhshan, S. M., & Baradaran, B. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2015.16.6.2129 · Cited by 611 · see citing works

RIPK1 Blocks Early Postnatal Lethality Mediated by Caspase-8 and RIPK3

Dillon, C. P., Weinlich, R., Rodriguez, D. A., Cripps, J. G., Quarato, G., Gurung, P., Verbist, K. C., Brewer, T. L., Llambi, F., Gong, Y.-N., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.018 · Cited by 562 · see citing works

Cellular and Molecular Mechanisms of Liver Injury

Malhi, H., & Gores, G. J. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.03.002 · Cited by 559 · see citing works

RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis

Dannappel, M., Vlantis, K., Kumari, S., Polykratis, A., Kim, C., Wachsmuth, L., Eftychi, C., Lin, J., Corona, T., Hermance, N., et al. (2014) · Nature · doi:10.1038/nature13608 · Cited by 534 · see citing works

c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor α (TNFα)-induced NF-κB Activation

Varfolomeev, E. E., Goncharov, T., Fedorova, A. V., Dynek, J. N., Zobel, K., Deshayes, K., Fairbrother, W. J., & Vucic, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800128200 · Cited by 554 · see citing works

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Mahoney, D. J., Cheung, H. H., Mrad, R. L., Plenchette, S., Simard, C., Enwere, E., Arora, V., Mak, T. W., Lacasse, E. C., Waring, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711122105 · Cited by 540 · see citing works

Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases

Strasser, A., Cory, S., & Adams, J. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.307 · Cited by 530 · see citing works

IAP-targeted therapies for cancer

LaCasse, E. C., Mahoney, D. J., Cheung, H. H., Plenchette, S., Baird, S. D., & Korneluk, R. G. (2008) · Oncogene · doi:10.1038/onc.2008.302 · Cited by 524 · see citing works

Ubiquitination in the regulation of inflammatory cell death and cancer

Cockram, P. E., Kist, M., Prakash, S., Chen, S., Wertz, I. E., & Vucic, D. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00708-5 · Cited by 520 · see citing works

The TNF Family of Ligands and Receptors: Communication Modules in the Immune System and Beyond

Dostert, C., Grusdat, M., Letellier, E., & Brenner, D. (2018) · Physiological Reviews · doi:10.1152/physrev.00045.2017 · Cited by 502 · see citing works

Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin

Lightfield, K. L., Persson, J., Brubaker, S. W., Witte, C. E., von Moltke, J., Dunipace, E. A., Henry, T., Sun, Y., Cado, D., Dietrich, W. F., et al. (2008) · Nature Immunology · doi:10.1038/ni.1646 · Cited by 487 · see citing works

Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation

Vince, J. E., Wong, W. W.-L., Gentle, I., Lawlor, K. E., Allam, R., O'Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.012 · Cited by 491 · see citing works

Expanding TRAF function: TRAF3 as a tri-faced immune regulator

Häcker, H., Tseng, P.-H., & Karin, M. (2011) · Nature Reviews Immunology · doi:10.1038/nri2998 · Cited by 471 · see citing works

XIAP discriminates between type I and type II FAS-induced apoptosis

Jost, P. J., Grabow, S., Gray, D., McKenzie, M. D., Nachbur, U., Huang, D. C. S., Bouillet, P., Thomas, H. E., Borner, C., Silke, J., et al. (2009) · Nature · doi:10.1038/nature08229 · Cited by 482 · see citing works

Caspases and Kinases in a Death Grip

Kurokawa, M., & Kornbluth, S. A. (2009) · Cell · doi:10.1016/j.cell.2009.08.021 · Cited by 476 · see citing works

HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins

Buckley, D. L., Raina, K., Darricarrere, N., Hines, J., Gustafson, J. L., Smith, I. E., Miah, A. H., Harling, J. D., & Crews, C. M. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00442 · Cited by 488 · see citing works

The Role of Ubiquitin in NF-κB Regulatory Pathways

Skaug, B. A., Jiang, X., & Chen, Z. J. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.102750 · Cited by 471 · see citing works

TRAF molecules in cell signaling and in human diseases

Xie, P. (2013) · Journal of Molecular Signaling · doi:10.1186/1750-2187-8-7 · Cited by 467 · see citing works

The p53 orchestra: Mdm2 and Mdmx set the tone

Wade, M., Wang, Y. V., & Wahl, G. M. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.009 · Cited by 450 · see citing works

IAPs: What's in a Name?

Srinivasula, S. M., & Ashwell, J. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.008 · Cited by 450 · 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

Mitochondria and cell death-associated inflammation

Vringer, E., & Tait, S. W. G. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01094-w · Cited by 441 · see citing works

Drugging the undruggables: exploring the ubiquitin system for drug development

Huang, X., & Dixit, V. M. (2016) · Cell Research · doi:10.1038/cr.2016.31 · Cited by 427 · see citing works

Hepatocyte Death: A Clear and Present Danger

Malhi, H., Guicciardi, M. E., & Gores, G. J. (2010) · Physiological Reviews · doi:10.1152/physrev.00061.2009 · Cited by 477 · see citing works

Many stimuli pull the necrotic trigger, an overview

Vanlangenakker, N., Berghe, T. V., & Vandenabeele, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.164 · Cited by 407 · see citing works

RIPK1 inhibits ZBP1-driven necroptosis during development

Newton, K., Wickliffe, K. E., Maltzman, A., Dugger, D. L., Strasser, A., Pham, V. C., Lill, J. R., Roose-Girma, M., Warming, S., Solon, M., et al. (2016) · Nature · doi:10.1038/nature20559 · Cited by 390 · see citing works

Targeting apoptotic caspases in cancer

Boice, A., & Bouchier‐Hayes, L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118688 · Cited by 402 · see citing works

Extrinsic and intrinsic apoptosis activate pannexin‐1 to drive NLRP3 inflammasome assembly

Chen, K. W., Demarco, B., Heilig, R., Shkarina, K., Boettcher, A., Farady, C. J., Pelczar, P., & Brož, P. (2019) · The EMBO Journal · doi:10.15252/embj.2019101638 · Cited by 389 · see citing works

Immunogenic cell death in cancer: targeting necroptosis to induce antitumour immunity

Meier, P., Legrand, A. J., Adam, D., & Silke, J. (2024) · Nature reviews. Cancer · doi:10.1038/s41568-024-00674-x · Cited by 405 · see citing works

The NF-κB activation pathways, emerging molecular targets for cancer prevention and therapy

Lin, Y., Bai, L., Chen, W., & Xu, S. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903431069 · Cited by 380 · see citing works

MLKL, the Protein that Mediates Necroptosis, Also Regulates Endosomal Trafficking and Extracellular Vesicle Generation

Yoon, S., Kovalenko, A., Bogdanov, K., & Wallach, D. (2017) · Immunity · doi:10.1016/j.immuni.2017.06.001 · Cited by 368 · see citing works

Fas death receptor signalling: roles of Bid and XIAP

Kaufmann, T., Strasser, A., & Jost, P. J. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.121 · Cited by 374 · 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

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

Programmed Necrosis in the Cross Talk of Cell Death and Inflammation

Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 350 · see citing works

cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

Vanlangenakker, N., Vanden Berghe, T., Bogaert, P., Laukens, B., Zobel, K., Deshayes, K., Vucic, D., Fulda, S., Vandenabeele, P., & Bertrand, M. J. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.138 · Cited by 339 · 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

Tumor Necrosis Factor Receptor-Associated Factor Regulation of Nuclear Factor κB and Mitogen-Activated Protein Kinase Pathways

Shi, J., & Sun, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01849 · Cited by 330 · see citing works

Degradation of proteins by PROTACs and other strategies

Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335 · see citing works

Cell death pathways: intricate connections and disease implications

Kist, M., & Vucic, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106700 · Cited by 328 · see citing works

Return to homeostasis: downregulation of NF-κB responses

Ruland, J. (2011) · Nature Immunology · doi:10.1038/ni.2055 · Cited by 321 · see citing works

CYLD Deubiquitinates RIP1 in the TNFα-Induced Necrosome to Facilitate Kinase Activation and Programmed Necrosis

Moquin, D. M., McQuade, T., & Chan, F. K.-M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076841 · Cited by 320 · see citing works

New insights into NF-κB regulation and function

Sun, S., & Ley, S. C. (2008) · Trends in Immunology · doi:10.1016/j.it.2008.07.003 · Cited by 320 · see citing works

MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death

Jaco, I., Annibaldi, A., Lalaoui, N., Wilson, R., Tenev, T., Laurien, L., KIM, C. S., Jamal, K., John, S. W., Liccardi, G., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.003 · Cited by 320 · 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

Necroptosis molecular mechanisms: Recent findings regarding novel necroptosis regulators

Seo, J., Nam, Y., Kim, S., Oh, D., & Song, J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00634-7 · Cited by 310 · see citing works

Chemistries of bifunctional PROTAC degraders

Cao, C., He, M., Wang, L., He, Y., & Rao, Y. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00220e · Cited by 313 · see citing works

Mechanisms of proteasome inhibitor action and resistance in cancer

McConkey, D. J., & Zhu, K. (2008) · Drug Resistance Updates · doi:10.1016/j.drup.2008.08.002 · Cited by 309 · see citing works

Noncanonical NF-κB Signaling in Health and Disease

Cildir, G., Low, K. C., & Tergaonkar, V. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.03.002 · Cited by 301 · see citing works

Small-Molecule Modulation of Protein Homeostasis.

Burslem, G., & Crews, C. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00077 · Cited by 256 · see citing works

Cell-to-cell variation in p53 dynamics leads to fractional killing.

Paek, A. L., Liu, J. C., Loewer, A., Forrester, W. C., & Lahav, G. (2016) · Cell · doi:10.1016/j.cell.2016.03.025 · Cited by 292 · see citing works

IAP Regulation of Metastasis

Mehrotra, S., Languino, L. R., Raskett, C. M., Mercurio, A. M., Dohi, T., & Altieri, D. C. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.021 · Cited by 288 · see citing works

The DNA damage-induced cell death response: a roadmap to kill cancer cells

Matt, S., & Hofmann, T. G. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2130-4 · Cited by 288 · see citing works

TNFR1‐induced activation of the classical NF‐κB pathway

Wajant, H., & Scheurich, P. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08015.x · Cited by 287 · see citing works

XIAP mediates NOD signaling via interaction with RIP2

Krieg, A. H., Correa, R. G., Garrison, J. B., Negrate, G. L., Welsh, K., Huang, Z., Knoefel, W. T., & Reed, J. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907131106 · Cited by 287 · see citing works

Overcoming chemotherapy drug resistance by targeting inhibitors of apoptosis proteins (IAPs)

Rathore, R., McCallum, J. E., Varghese, E., Florea, A.-M., & Büsselberg, D. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1375-1 · Cited by 278 · see citing works

Regulation of cell death and autophagy by IKK and NF‐κB: critical mechanisms in immune function and cancer

Baldwin, A. S. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01095.x · 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

Ubiquitination: Friend and foe in cancer

Mansour, M. A. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.06.001 · Cited by 273 · see citing works

Caspase-8 Acts in a Non-enzymatic Role as a Scaffold for Assembly of a Pro-inflammatory “FADDosome” Complex upon TRAIL Stimulation

Henry, C. M., & Martin, S. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.022 · Cited by 267 · see citing works

Tumor Necrosis Factor Receptors: Pleiotropic Signaling Complexes and Their Differential Effects

Gough, P., & Myles, I. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.585880 · Cited by 270 · see citing works

XIAP Restricts TNF- and RIP3-Dependent Cell Death and Inflammasome Activation

Yabal, M., Müller, N., Adler, H., Knies, N., Groß, C. J., Damgaard, R. B., Kanegane, H., Ringelhan, M., Kaufmann, T., Heikenwälder, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.008 · Cited by 255 · see citing works

Regulation of apoptosis in Drosophila

Steller, H. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.50 · Cited by 268 · see citing works

Regulation of the human catalytic subunit of telomerase (hTERT)

Daniel, M. G., Peek, G. W., & Tollefsbol, T. O. (2012) · Gene · doi:10.1016/j.gene.2012.01.095 · Cited by 265 · see citing works

Herpes Simplex Virus Suppresses Necroptosis in Human Cells

Guo, H., Omoto, S., Harris, P. A., Finger, J. N., Bertin, J., Gough, P. J., Kaiser, W. J., & Mocarski, E. S. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.01.003 · Cited by 261 · see citing works

Opportunities in discovery and delivery of anticancer drugs targeting mitochondria and cancer cell metabolism☆

Pathania, D., Millard, M., & Neamati, N. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.010 · Cited by 265 · see citing works

Mitochondrial permeabilization engages NF-κB-dependent anti-tumour activity under caspase deficiency

Giampazolias, E., Zunino, B., Dhayade, S., Bock, F., Cloix, C., Cao, K., Roca, A., Lopez, J., Ichim, G., Proïcs, E., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3596 · Cited by 258 · see citing works

Abstract 137: Targeting IAPs: NF-κB signaling pathways play a critical role in IAP antagonist induced apoptosis

Varfolomeev, E. E., Goncharov, T., & Vucic, D. (2010) · Cancer Research · doi:10.1158/1538-7445.am10-137

(Un)expected roles of c-IAPs in apoptotic and NFκB signaling pathways

Varfolomeev, E. E., & Vucic, D. (2008) · Cell Cycle · doi:10.4161/cc.7.11.5959 · Cited by 125 · see citing works

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 · see citing works

Ubiquitination profiling identifies sensitivity factors for IAP antagonist treatment

Varfolomeev, E. E., Izrael-Tomasevic, A., Yu, K., Bustos, D. J., Goncharov, T., Belmont, L. D., Masselot, A., Bakalarski, C. E., Kirkpatrick, D. S., & Vucic, D. (2014) · Biochemical Journal · doi:10.1042/bj20141195 · Cited by 9 · see citing works

IAP Proteins and Their Therapeutic Potential

Vucic, D. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9302-0_5 · Cited by 2 · see citing works