The E3 Ubiquitin Ligase Itch Couples JNK Activation to TNFα-induced Cell Death by Inducing c-FLIPL Turnover

Phosphorylation meets ubiquitination: the control of NF-κB activity

Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626

A Third-Generation Lentivirus Vector with a Conditional Packaging System

Dull, T., Zufferey, R., Kelly, M., Mandel, R. J., Nguyen, M., Trono, D., & Naldini, L. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8463-8471.1998 · Cited by 3,341

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

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

NF-κB at the crossroads of life and death

Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709

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

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules.

Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., & Goldberg, A. L. (1994) · Cell · doi:10.1016/s0092-8674(94)90462-6 · Cited by 2,524

Tumor necrosis factor signaling

Wajant, H., Pfizenmaier, K., & Scheurich, P. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401189 · Cited by 2,422

Dissection of TNF Receptor 1 Effector Functions: JNK Activation Is Not Linked to Apoptosis While NF-κB Activation Prevents Cell Death

Liu, Z.-G., Hsu, H., Goeddel, D. V., & Karin, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81375-6 · Cited by 1,937

Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases

Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792

CD95's deadly mission in the immune system

Krammer, P. H. (2000) · Nature · doi:10.1038/35037728 · Cited by 1,710

The proteasome: a suitable antineoplastic target

Adams, J. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1361 · Cited by 1,214

A T cell-dependent experimental liver injury in mice inducible by concanavalin A.

Tiegs, G., Hentschel, J., & Wendel, A. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115836 · Cited by 1,077

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

Mule/ARF-BP1, a BH3-Only E3 Ubiquitin Ligase, Catalyzes the Polyubiquitination of Mcl-1 and Regulates Apoptosis

Zhong, Q., Gao, W., Du, F., & Wang, X. (2005) · Cell · doi:10.1016/j.cell.2005.06.009 · Cited by 844

NF-κB Signals Induce the Expression of c-FLIP

Micheau, O., Lens, S. M. A., Gaide, O., Alevizopoulos, K., & Tschopp, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.16.5299-5305.2001 · Cited by 809

Induction of gadd45β by NF-κB downregulates pro-apoptotic JNK signalling

De Smaele, E., Zazzeroni, F., Papa, S., Nguyen, D. U., Jin, R., Jones, J., Cong, R., & Franzoso, G. (2001) · Nature · doi:10.1038/35104560 · Cited by 732

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

Ferritin heavy chain upregulation by NF-κB inhibits TNFα-induced apoptosis by suppressing reactive oxygen species

Pham, C. G., Bubici, C., Zazzeroni, F., Papa, S., Jones, J., Alvarez, K., Jayawardena, S., De Smaele, E., Cong, R., Beaumont, C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.017 · Cited by 663

A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia

Borsello, T., Clarke, P. G. H., Hirt, L., Vercelli, A., Repici, M., Schorderet, D. F., Bogousslavsky, J., & Bonny, C. (2003) · Nature Medicine · doi:10.1038/nm911 · Cited by 658

Cellular FLICE-inhibitory Protein Splice Variants Inhibit Different Steps of Caspase-8 Activation at the CD95 Death-inducing Signaling Complex

Krueger, A., Schmitz, I., Baumann, S., Krammer, P. H., & Kirchhoff, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101780200 · Cited by 565

A JNK-Dependent Pathway Is Required for TNFα-Induced Apoptosis

Deng, Y., Ren, X., Yang, L., Lin, Y., & Wu, X. (2003) · Cell · doi:10.1016/s0092-8674(03)00757-8 · Cited by 553

FLICE-Inhibitory Proteins: Regulators of Death Receptor-Mediated Apoptosis

Krueger, A., Baumann, S., Krammer, P. H., & Kirchhoff, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8247-8254.2001 · Cited by 548

Requirement for Casper (c-FLIP) in Regulation of Death Receptor–Induced Apoptosis and Embryonic Development

Yeh, W.-C., Itie, A., Elia, A. J., Ng, M., Shu, H.-B., Wakeham, A., Mirtsos, C., Suzuki, N., Bonnard, M., Goeddel, D. V., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80214-9 · Cited by 515

Macrophage Apoptosis by Anthrax Lethal Factor Through p38 MAP Kinase Inhibition

Park, J. M., Greten, F. R., Li, Z., & Karin, M. (2002) · Science · doi:10.1126/science.1073163 · Cited by 500

Tumor Necrosis Factor

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

Galactosamine hepatitis: Key role of the nucleotide deficiency period in the pathogenesis of cell injury and cell death

Decker, K., & KEPPLER, D. O. R. (2005) · Springer eBooks · doi:10.1007/bfb0027661 · Cited by 446

Jun Turnover Is Controlled Through JNK-Dependent Phosphorylation of the E3 Ligase Itch

Gao, M., Labuda, T., Xia, Y., Gallagher, E. D., Fang, D., Liu, Y., & Karin, M. (2004) · Science · doi:10.1126/science.1099414 · Cited by 397

Regulation of lymphocyte proliferation and death by flip

Thome, M., & Tschopp, J. (2001) · Nature reviews. Immunology · doi:10.1038/35095508 · Cited by 375

JNK1 Is Required for Maintenance of Neuronal Microtubules and Controls Phosphorylation of Microtubule-Associated Proteins

Chang, L., Jones, Y., Ellisman, M. H., Goldstein, L. S. B., & Karin, M. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00094-7 · Cited by 375

Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation

Fang, D., Elly, C., Gao, B., Fang, N., Altman, Y., Joazeiro, C. A. P., Hunter, T. R., Copeland, N. G., Jenkins, N. A., & Liu, Y. (2002) · Nature Immunology · doi:10.1038/ni763 · Cited by 341

Life And Death Decisions

Muppidi, J. R., Tschopp, J., & Siegel, R. M. (2004) · Immunity · doi:10.1016/j.immuni.2004.10.001 · Cited by 339

IKKβ Is Required for Prevention of Apoptosis Mediated by Cell-Bound but Not by Circulating TNFα

Maeda, S., Chang, L., Li, Z.-W., Luo, J.-L., Leffert, H., & Karin, M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00301-7 · Cited by 286

c-FLIPR, a New Regulator of Death Receptor-induced Apoptosis

Golks, A., Brenner, D., Fritsch, C., Krammer, P. H., & Lavrik, I. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414425200 · Cited by 281

Linking JNK signaling to NF-κB: a key to survival

Papa, S., Zazzeroni, F., Pham, C. G., Bubici, C., & Franzoso, G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01483 · Cited by 277

c-Jun N-Terminal Protein Kinase 1 (JNK1), but Not JNK2, Is Essential for Tumor Necrosis Factor Alpha-Induced c-Jun Kinase Activation and Apoptosis

Liu, J., Minemoto, Y., & Lin, A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10844-10856.2004 · Cited by 201

The ubiquitin system: pathogenesis of human diseases and drug targeting

Ciechanover, A. J., & Schwartz, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.018 · Cited by 171

TCR-Mediated Up-Regulation of c-FLIPshort Correlates with Resistance Toward CD95-Mediated Apoptosis by Blocking Death-Inducing Signaling Complex Activity

Kirchhoff, S., Müller, W. W., Krueger, A., Schmitz, I., & Krammer, P. H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.11.6293 · Cited by 131

Itch E3 Ligase-Mediated Regulation of TGF-β Signaling by Modulating Smad2 Phosphorylation

Bai, Y., Yang, C., Hu, K., Elly, C., & Liu, Y. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.021 · Cited by 123

The JNKK2-JNK1 fusion protein acts as a constitutively active c-Jun kinase that stimulates c-Jun transcription activity

Zheng, C., Xiang, J., Hunter, T., & Lin, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28966 · Cited by 110

Activation of the Ras-related GTPase Rap1 by thymocyte TCR engagement and during selection

(2000) · Pure Amsterdam UMC · doi:10.1002/1521-4141(200010)30:10 · Cited by 3

Immunity, Inflammation, and Cancer

Grivennikov, S. I., Greten, F. R., & Karin, M. (2010) · Cell · doi:10.1016/j.cell.2010.01.025 · Cited by 10,755

Nuclear factor-κB in cancer development and progression

Karin, M. (2006) · Nature · doi:10.1038/nature04870 · Cited by 3,519

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340

Signal integration by JNK and p38 MAPK pathways in cancer development

Wagner, E. F., & Nebreda, Á. R. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2694 · Cited by 2,635

Targeting NF-κB pathway for the therapy of diseases: mechanism and clinical study

Yu, H., Lin, L., Zhang, Z., Zhang, H., & Hu, H. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00312-6 · Cited by 2,329

Research Highlights

(2006) · Nature Immunology · doi:10.1038/ni0406-373

An antiapoptotic protein, c‐FLIPL, directly binds to MKK7 and inhibits the JNK pathway

Nakajima, A., Komazawa‐Sakon, S., Takekawa, M., Sasazuki, T., Yeh, W., Yagita∥, H., Okumura, K., & Nakano, H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601423 · Cited by 94

Tumor Necrosis Factor (TNF) Receptor-associated Factor 7 Is Required for TNFα-induced Jun NH2-terminal Kinase Activation and Promotes Cell Death by Regulating Polyubiquitination and Lysosomal Degradation of c-FLIP Protein

Scudiero, I., Zotti, T., Ferravante, A., Vessichelli, M., Reale, C., Masone, M. C., Leonardi, A., Vito, P., & Stilo, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.300137 · Cited by 48

A Five-Year Itch in TNF-α Cytotoxicity: The Time Factor Determines JNK Action

Lin, A. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.02.006 · Cited by 19

The Absence of NF-κB-Mediated Inhibition of c-Jun N-Terminal Kinase Activation Contributes to Tumor Necrosis Factor Alpha-Induced Apoptosis

Tang, F., Tang, G., Xiang, J., Dai, Q., Rosner, M. R., & Lin, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8571-8579.2002 · Cited by 145