Ubiquitin, TAK1 and IKK: is there a connection?

NF-κB: Ten Years After

Baeuerle, P. A., & Baltimore, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81318-5 · Cited by 3,002 · see citing works

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125 · see citing works

Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain

Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872 · 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

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

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

The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway

Ninomiya‐Tsuji, J., Kishimoto, K., Hiyama, A., Inoue, J., Cao, Z., & Matsumoto, K. (1999) · Nature · doi:10.1038/18465 · Cited by 1,187 · see citing works

The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal

Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102 · see citing works

The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination

Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., & Courtois, G. (2003) · Nature · doi:10.1038/nature01802 · Cited by 1,018 · see citing works

CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members

Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., & Mosialos, G. (2003) · Nature · doi:10.1038/nature01803 · Cited by 964 · see citing works

Site-Specific Phosphorylation of IκBα by a Novel Ubiquitination-Dependent Protein Kinase Activity

Chen, Z. J., Parent, L. A., & Maniatis, T. (1996) · Cell · doi:10.1016/s0092-8674(00)81064-8 · Cited by 958 · see citing works

Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB

Brummelkamp, T. R., Nijman, S. M. B., Dirac, A. M. G., & Bernards, R. (2003) · Nature · doi:10.1038/nature01811 · Cited by 947 · see citing works

Noncanonical MMS2-Encoded Ubiquitin-Conjugating Enzyme Functions in Assembly of Novel Polyubiquitin Chains for DNA Repair

Hofmann, R. M., & Pickart, C. M. (1999) · Cell · doi:10.1016/s0092-8674(00)80575-9 · Cited by 815 · see citing works

Early Lethality, Functional NF-κB Activation, and Increased Sensitivity to TNF-Induced Cell Death in TRAF2-Deficient Mice

Yeh, W., Shahinian, A., Speiser, D. E., Kraunus, J., Billia, F., Wakeham, A. C., de la Pompa, J. L., Ferrick, D. A., Hum, B., Iscove, N. N., et al. (1997) · Immunity · doi:10.1016/s1074-7613(00)80391-x · Cited by 798 · see citing works

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

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

Bcl10 activates the NF-κB pathway through ubiquitination of NEMO

Zhou, H., Wertz, I. E., O’Rourke, K. M., Ultsch, M. H., Seshagiri, S., Eby, M. T., Xiao, W., & Dixit, V. M. (2003) · Nature · doi:10.1038/nature02273 · Cited by 527 · see citing works

Recruitment of TNF Receptor 1 to Lipid Rafts Is Essential for TNFα-Mediated NF-κB Activation

Legler, D. F., Micheau, O., Doucey, M., Tschopp, J., & Bron, C. (2003) · Immunity · doi:10.1016/s1074-7613(03)00092-x · Cited by 464 · see citing works

Recruitment of the IKK Signalosome to the p55 TNF Receptor

Zhang, S. Q., Kovalenko, A., Cantarella, G., & Wallach, D. (2000) · Immunity · doi:10.1016/s1074-7613(00)80183-1 · Cited by 456 · see citing works

TRAF2 Is Essential for JNK but Not NF-κB Activation and Regulates Lymphocyte Proliferation and Survival

Lee, S. Y., Reichlin, A., Santana, A., Sokol, K. A., Nussenzweig, M. C., & Choi, Y. (1997) · Immunity · doi:10.1016/s1074-7613(00)80390-8 · Cited by 445 · see citing works

Constitutive NF-κB activation by the t(11;18)(q21;q21) product in MALT lymphoma is linked to deregulated ubiquitin ligase activity

Zhou, H., Du, M., & Dixit, V. M. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.012 · Cited by 140 · see citing works

Cutting Edge: Profound Defect in T Cell Responses in TNF Receptor-Associated Factor 2 Dominant Negative Mice

Cannons, J. L., Bertram, E. M., & Watts, T. H. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.6.2828 · Cited by 25 · 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

Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction

Haas, T. L., Emmerich, C. H., Gerlach, B., Schmukle, A. C., Cordier, S. M., Rieser, E., Feltham, R., Vince, J. E., Warnken, U. H., Wenger, T., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.013 · Cited by 768 · see citing works

The Molecular Bases of Training Adaptation

Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756 · see citing works

Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway

Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674 · 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

Direct activation of protein kinases by unanchored polyubiquitin chains

Xia, Z.-P., Sun, L., Chen, X., Pineda, G., Jiang, X., Adhikari, A., Zeng, W., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature08247 · Cited by 570 · see citing works

Ubiquitin-mediated activation of TAK1 and IKK

Adhikari, A., Xu, M., & Chen, Z. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210413 · Cited by 455 · see citing works

NF-κB in inflammation and renal diseases

Zhang, H., & Sun, S.-C. (2015) · Cell & Bioscience · doi:10.1186/s13578-015-0056-4 · Cited by 383 · see citing works

Cell type-specific function of TAK1 in innate immune signaling

Alagbala, A. A., Wang, H. Y., & Wang, R. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.03.007 · Cited by 372 · see citing works

IκB kinase β (IKKβ/IKK2/IKBKB)—A key molecule in signaling to the transcription factor NF-κB

Schmid, J. A., & Birbach, A. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.006 · Cited by 260 · see citing works

Role of nuclear factor κB in cardiovascular health and disease

der Heiden, K. V., Cuhlmann, S., Luong, L. A., Zakkar, M., & Evans, P. C. (2010) · Clinical Science · doi:10.1042/cs20090557 · Cited by 236 · see citing works

ATM- and NEMO-Dependent ELKS Ubiquitination Coordinates TAK1-Mediated IKK Activation in Response to Genotoxic Stress

Wu, Z.-H., Wong, E. T., Shi, Y., Niu, J., Chen, Z. J., Miyamoto, S., & Tergaonkar, V. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.010 · Cited by 207 · see citing works

Inhibition of MALT1 protease activity is selectively toxic for activated B cell–like diffuse large B cell lymphoma cells

Ferch, U., Kloo, B., Gewies, A., Pfänder, V., Düwel, M., Peschel, C., Krappmann, D., & Ruland, J. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20091167 · Cited by 202 · see citing works

Cell Signaling and Function Organized by PB1 Domain Interactions

Moscat, J., Díaz-Meco, M. T., Albert, A., & Campuzano, S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.002 · Cited by 195 · see citing works

Roles of NF-κB in health and disease: mechanisms and therapeutic potential

Wong, E. T., & Tergaonkar, V. (2009) · Clinical Science · doi:10.1042/cs20080502 · Cited by 195 · see citing works

Exploitation of Eukaryotic Ubiquitin Signaling Pathways by Effectors Translocated by Bacterial Type III and Type IV Secretion Systems

Angot, A., Vergunst, A. C., Genin, S., & Peeters, N. M. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030003 · Cited by 176 · see citing works

Coordinating TLR‐activated signaling pathways in cells of the immune system

Banerjee, A., & Gerondakis, S. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100098 · Cited by 163 · see citing works

TAK1-dependent Signaling Requires Functional Interaction with TAB2/TAB3

Besse, A., Lamothe, B., Campos, A. D., Webster, W. K., Maddineni, U., Lin, S., Wu, H., & Darnay, B. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608867200 · Cited by 145 · see citing works

A newly discovered post-translational modification – the acetylation of serine and threonine residues

Mukherjee, S., Hao, Y.-H., & Orth, K. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.03.007 · Cited by 141 · see citing works

The Drosophila Inhibitor of Apoptosis Protein DIAP2 Functions in Innate Immunity and Is Essential To Resist Gram-Negative Bacterial Infection

Leulier, F., Lhocine, N., Lemaître, B., & Meier, P. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00548-06 · Cited by 136 · see citing works

Current concepts of IgE regulation and impact of genetic determinants

Potaczek, D. P., & Kabesch, M. (2012) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2011.03953.x · Cited by 124 · see citing works

Heat Shock Protein 27 Functions in Inflammatory Gene Expression and Transforming Growth Factor-β-activated Kinase-1 (TAK1)-mediated Signaling

Alford, K. A., Glennie, S. J., Turrell, B. R., Rawlinson, L. M., Saklatvala, J., & Dean, J. L. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610987200 · Cited by 123 · see citing works

Phosphorylation and ubiquitination of the IκB kinase complex by two distinct signaling pathways

Shambharkar, P. B., Blonska, M., Pappu, B. P., Li, H., You, Y., Sakurai, H., Darnay, B. G., Hara, H., Penninger, J. M., & Lin, X. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601622 · Cited by 122 · see citing works

Ubiquitin-conjugating enzyme Ubc13 is a critical component of TNF receptor-associated factor (TRAF)-mediated inflammatory responses

Fukushima, T., Matsuzawa, S., Kress, C. L., Bruey, J. M., Krajewska, M., Lefebvre, S., Zapata, J. M., Ronai, Z. A., & Reed, J. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700548104 · Cited by 114 · see citing works

Lipopolysaccharide-Induced Increase in Intestinal Permeability Is Mediated by TAK-1 Activation of IKK and MLCK/MYLK Gene

Nighot, M., Rawat, M., Al–Sadi, R., Castillo, E. F., Nighot, P. K., & Ma, T. Y. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2018.12.016 · Cited by 111 · see citing works

Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes

Ku, C. S., Pham, T. X., Park, Y., Kim, B., Shin, M. S., Kang, I., & Lee, J. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.01.018 · Cited by 109 · see citing works

USP18 protects against hepatic steatosis and insulin resistance through its deubiquitinating activity

An, S., Zhao, L., She, Z., Wang, S., Zhang, K., Yu, Q., Zheng, J., Zhang, X., Zhu, X., Bao, R., et al. (2017) · Hepatology · doi:10.1002/hep.29375 · Cited by 104 · see citing works

TAK1 Regulates Reactive Oxygen Species and Cell Death in Keratinocytes, Which Is Essential for Skin Integrity

Omori, E., Morioka, S., Matsumoto, K., & Ninomiya‐Tsuji, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804513200 · Cited by 99 · see citing works

TAK1 Is a Central Mediator of NOD2 Signaling in Epidermal Cells

Kim, J., Omori, E., Matsumoto, K., Núñez, G., & Ninomiya‐Tsuji, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704746200 · Cited by 98 · see citing works

Sustained oxidative stress inhibits NF-κB activation partially via inactivating the proteasome

Wu, M., Bian, Q., Liu, Y., Fernandes, A. F., Taylor, A., Pereira, P., & Shang, F. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.021 · Cited by 97 · see citing works

Transforming Growth Factor-β (TGF-β1) Activates TAK1 via TAB1-mediated Autophosphorylation, Independent of TGF-β Receptor Kinase Activity in Mesangial Cells

Kim, S. I., Kwak, J. H., Na, H.-J., Kim, J. K., Ding, Y., & Choi, M. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007146 · Cited by 87 · see citing works

Leishmania donovani Exploits Host Deubiquitinating Enzyme A20, a Negative Regulator of TLR Signaling, To Subvert Host Immune Response

Srivastav, S., Kar, S., Chande, A. G., Mukhopadhyaya, R., & Das, P. K. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102845 · Cited by 85 · see citing works

TAK1 lysine 158 is required for TGF-β-induced TRAF6-mediated Smad-independent IKK/NF-κB and JNK/AP-1 activation

Mao, R., Fan, Y., Mou, Y., Zhang, H., Fu, S., & Yang, J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.09.006 · Cited by 73 · see citing works

Retroviral oncoprotein Tax deregulates NF‐κB by activating Tak1 and mediating the physical association of Tak1–IKK

Wu, X., & Sun, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400931 · Cited by 72 · see citing works

Glutathione Depletion Down-regulates Tumor Necrosis Factor α-induced NF-κB Activity via IκB Kinase-dependent and -independent Mechanisms

Lou, H., & Kaplowitz, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706145200 · Cited by 71 · see citing works

TAK1-binding Protein 1, TAB1, Mediates Osmotic Stress-induced TAK1 Activation but Is Dispensable for TAK1-mediated Cytokine Signaling

Inagaki, M., Omori, E., Kim, J.-Y., Komatsu, Y., Scott, G., Ray, M. K., Yamada, G., Matsumoto, K., Mishina, Y., & Ninomiya-Tsuji, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807574200 · Cited by 68 · see citing works

HIV-1 Vpr stimulates NF-κB and AP-1 signaling by activating TAK1

Liu, R., Lin, Y., Jia, R., Geng, Y., Liang, C., Tan, J., & Qiao, W. (2014) · Retrovirology · doi:10.1186/1742-4690-11-45 · Cited by 66 · see citing works

Denbinobin inhibits nuclear factor-κB and induces apoptosis via reactive oxygen species generation in human leukemic cells

Sánchez‐Duffhues, G., Calzado, M. A., de Vinuesa, A. G., Appendino, G., Fiebich, B. L., Loock, U., Lefarth‐Risse, A., Krohn, K., & Muñóz, E. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.01.004 · Cited by 65 · see citing works

Tumor Necrosis Factor-α Augments Matrix Metalloproteinase-9 Production in Skeletal Muscle Cells through the Activation of Transforming Growth Factor-β-activated Kinase 1 (TAK1)-dependent Signaling Pathway

Srivastava, A. K., Qin, X., Wedhas, N., Arnush, M., Linkhart, T. A., Chadwick, R. B., & Kumar, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705329200 · Cited by 63 · see citing works

Human Trim5α has additional activities that are uncoupled from retroviral capsid recognition

Tareen, S. U., & Emerman, M. (2010) · Virology · doi:10.1016/j.virol.2010.09.018 · Cited by 63 · see citing works

Peli: a family of signal-responsive E3 ubiquitin ligases mediating TLR signaling and T-cell tolerance

Jin, W., Chang, M., & Sun, S. (2012) · Cellular and Molecular Immunology · doi:10.1038/cmi.2011.60 · Cited by 60 · see citing works

Roles for the ubiquitin–proteasome pathway in protein quality control and signaling in the retina: Implications in the pathogenesis of age-related macular degeneration

Shang, F., & Taylor, A. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.04.001 · Cited by 60 · see citing works

Essential role of TAK1 in regulating mantle cell lymphoma survival

Buglio, D., Palakurthi, S. S., Byth, K. F., Vega, F., Toader, D., Saeh, J. C., Neelapu, S. S., & Younes, A. (2012) · Blood · doi:10.1182/blood-2011-07-369397 · Cited by 59 · see citing works

The Lysosomal Transmembrane Protein 9B Regulates the Activity of Inflammatory Signaling Pathways

Dodeller, F., Gottar, M., Huesken, D., Iourgenko, V., & Cenni, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801908200 · Cited by 58 · see citing works

Epithelial transforming growth factor β-activated kinase 1 (TAK1) is activated through two independent mechanisms and regulates reactive oxygen species

Omori, E., Inagaki, M., Mishina, Y. M., Matsumoto, K., & Ninomiya‐Tsuji, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116188109 · Cited by 55 · see citing works

TAB4 Stimulates TAK1-TAB1 Phosphorylation and Binds Polyubiquitin to Direct Signaling to NF-κB

Prickett, T. D., Ninomiya‐Tsuji, J., Broglie, P. M., Muratore‐Schroeder, T. L., Shabanowitz, J., Hunt, D. F., & Brautigan, D. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800943200 · Cited by 49 · see citing works

TAK1 inhibitor 5Z-7-oxozeaenol sensitizes neuroblastoma to chemotherapy

Fan, Y., Cheng, J., Vasudevan, S. A., Patel, R. H., Li, L., Xu, X. Y., Zhao, Y., Jia, W., Lu, F., Zhang, H., et al. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0864-0 · Cited by 49 · see citing works

TAK1 kinase determines TRAIL sensitivity by modulating reactive oxygen species and cIAP

Morioka, S., Omori, E., Kajino, T., Kajino‐Sakamoto, R., Matsumoto, K., & Ninomiya‐Tsuji, J. (2009) · Oncogene · doi:10.1038/onc.2009.110 · Cited by 49 · see citing works

Comprehending the complex connection between PKCβ, TAK1, and IKK in BCR signaling

Shinohara, H., & Kurosaki, T. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00836.x · Cited by 48 · see citing works

SIRT7 Regulates Lipopolysaccharide-Induced Inflammatory Injury by Suppressing the NF-κB Signaling Pathway

Chen, K., Li, L., Li, C., Wang, Y., Yang, F., Kuang, M., & Wang, G. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3187972 · Cited by 47 · see citing works

NF-κB as a Target for Oncogenic Viruses

Sun, S., & Cesarman, E. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_108 · Cited by 45 · see citing works

TAK1 ubiquitination regulates doxorubicin-induced NF-κB activation

Liang, L., Fan, Y., Cheng, J., Cheng, D., Zhao, Y., Cao, B., Ma, L., An, L., Jia, W., Xu, S., et al. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.003 · Cited by 44 · see citing works

NF-κB feedback control of JNK1 activation modulates TRPV1-induced increases in IL-6 and IL-8 release by human corneal epithelial cells.

Wang, Z., Yang, Y., Yang, H., Capó‐Aponte, J. E., Tachado, S. D., Wolosin, J. M., & Reinach, P. S. (2011) · PubMed Central · Cited by 43 · see citing works

Japonicone A Suppresses Growth of Burkitt Lymphoma Cells through Its Effect on NF-κB

Li, X., Yang, X., Liu, Y., Gong, N., Yao, W., Chen, P., Qin, J., Jin, H., Li, J., Chu, R., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-3258 · Cited by 42 · see citing works

DDX3 Participates in Translational Control of Inflammation Induced by Infections and Injuries

Ku, Y.-C., Lai, M.-H., Lo, C.-C., Cheng, Y., Qiu, J.-T. T., Tarn, W., & Lai, M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00285-18 · Cited by 42 · see citing works

Compound FLZ inhibits lipopolysaccharide-induced inflammatory effects via down-regulation of the TAK-IKK and TAK-JNK/p38MAPK pathways in RAW264.7 macrophages

Pang, H.-Y., Liu, G., & Liu, G.-T. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2008.29 · Cited by 39 · see citing works

Effect of High-Frequency Resistance Exercise on Adaptive Responses in Skeletal Muscle

Coffey, V. G., Reeder, D. W., Lancaster, G. I., Yeo, W. K., Febbraio, M. A., Yaspelkis, B. B., & Hawley, J. A. (2007) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31815729b6 · Cited by 39 · see citing works

Roles of TRAF6 in CD40 signaling

Hostager, B. S. (2007) · Immunologic Research · doi:10.1007/s12026-007-0082-3 · Cited by 39 · see citing works

TAK1 inhibition-induced RIP1-dependent apoptosis in murine macrophages relies on constitutive TNF-α signaling and ROS production

Wang, J.-S., Wu, D., Huang, D.-Y., & Lin, W. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0182-7 · Cited by 38 · see citing works

Pseudorabies Virus Infection of Epithelial Cells Leads to Persistent but Aberrant Activation of the NF-κB Pathway, Inhibiting Hallmark NF-κB-Induced Proinflammatory Gene Expression

Romero, N., Waesberghe, C. V., & Favoreel, H. W. (2020) · Journal of Virology · doi:10.1128/jvi.00196-20 · Cited by 34 · see citing works

SMYD2‐mediated TRAF2 methylation promotes the NF‐κB signaling pathways in inflammatory diseases

Wu, W., Wang, J., Xiao, C., Su, Z., Su, H., Zhong, W., Mao, J., Liu, X., & Zhu, Y. Z. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.591 · Cited by 33 · see citing works

IL-6 Induction by TNFα and IL-1β in an Osteoblast-Like Cell Line

Furia, A., Confalone, E., & D’Alessio, G. (2010) · International Journal of Biomedical Science · doi:10.59566/ijbs.2010.6135 · Cited by 33 · see citing works

Withaferin A disrupts ubiquitin-based NEMO reorganization induced by canonical NF-κB signaling

Jackson, S. S., Oberley, C. C., Hooper, C., Grindle, K. M., Wuerzberger‐Davis, S. M., Wolff, J., McCool, K. W., Rui, L., & Miyamoto, S. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.09.034 · Cited by 33 · see citing works

HSCARG downregulates NF-κB signaling by interacting with USP7 and inhibiting NEMO ubiquitination

Li, T., Guan, J., Li, S.-Z., Zhang, X., & Zheng, X. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.197 · Cited by 32 · see citing works

Epithelial Cell Death and Inflammation in Skin

Kumari, S., & Pasparakis, M. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_466 · Cited by 31 · see citing works

Tubocapsanolide A Inhibits Transforming Growth Factor-β-activating Kinase 1 to Suppress NF-κB-induced CCR7

Pan, M., Chang, H., Wu, Y., Huang, C.-C., & Hung, W.-C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806223200 · Cited by 31 · see citing works

Contraction-induced changes in TNFα and Akt-mediated signalling are associated with increased myofibrillar protein in rat skeletal muscle

Karagounis, L. G., Yaspelkis, B. B., Reeder, D. W., Lancaster, G. I., Hawley, J. A., & Coffey, V. G. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1427-5 · Cited by 30 · see citing works

POPX2 phosphatase regulates apoptosis through the TAK1-IKK-NF-κB pathway

Weng, T., & Koh, C.-G. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.443 · Cited by 29 · see citing works

Phosphorylation and Polyubiquitination of Transforming Growth Factor β-Activated Kinase 1 Are Necessary for Activation of NF-κB by the Kaposi's Sarcoma-Associated Herpesvirus G Protein-Coupled Receptor

Bottero, V., Kerur, N., Sadagopan, S., Patel, K., Sharma-Walia, N., & Chandran, B. (2010) · Journal of Virology · doi:10.1128/jvi.01911-10 · Cited by 29 · see citing works

PGC‐1β suppresses saturated fatty acid‐induced macrophage inflammation by inhibiting TAK1 activation

Chen, H., Liu, Y., Li, D., Song, J., & Xia, M. (2016) · IUBMB Life · doi:10.1002/iub.1470 · Cited by 28 · see citing works

HTLV-1 Tax-mediated TAK1 activation involves TAB2 adapter protein

Yu, Q., Minoda, Y., Yoshida, R., Yoshida, H., Iha, H., Kobayashi, T., Yoshimura, A., & Takaesu, G. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.172 · Cited by 28 · see citing works

Role of the Ubiquitin–Proteasome in Protein Quality Control and Signaling

Shang, F., & Taylor, A. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00010-9 · Cited by 28 · see citing works

Resistance exercise and skeletal muscle: protein synthesis, degradation, and controversies

Ji, F., Lee, H. S., & Kim, J.-H. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05832-z · Cited by 26 · see citing works

Activated Macrophage Survival Is Coordinated by TAK1 Binding Proteins

Mihaly, S. R., Morioka, S., Ninomiya‐Tsuji, J., & Takaesu, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094982 · Cited by 26 · see citing works

TAK1 inhibitor 5Z-7-oxozeaenol sensitizes cervical cancer to doxorubicin-induced apoptosis

Guan, S., Lu, J., Zhao, Y., Woodfield, S. E., Zhang, H., Xu, X. Y., Yu, Y., Zhao, J., Bieerkehazhi, S., Liang, H., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16895 · Cited by 25 · see citing works

TAK1 Is Required for Survival of Mouse Fibroblasts Treated with TRAIL, and Does So by NF-κB Dependent Induction of cFLIPL

Lluis, J. M., Nachbur, U., Cook, W. D., Gentle, I. E., Moujalled, D. M., Moulin, M., Wong, W. W.-L., Khan, N. R., Chau, D., Callus, B. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008620 · Cited by 24 · see citing works

Constitutive and Tumor Necrosis Factor-Alpha-Stimulated Activation of Nuclear Factor-KappaB in Immortalized Endometriotic Cells and Their Suppression by Trichostatin A

Wu, Y., Starzinski‐Powitz, A., & Guo, S. (2010) · Gynecologic and Obstetric Investigation · doi:10.1159/000279324 · Cited by 23 · see citing works

Overview of pyroptosis mechanism and in-depth analysis of cardiomyocyte pyroptosis mediated by NF-κB pathway in heart failure

Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117367 · Cited by 21 · see citing works

LncRNA linc00152/NF‐κB feedback loop promotes fibroblast‐like synovial cells inflammation in rheumatoid arthritis via regulating miR‐103a/TAK1 axis and YY1 expression

Zhang, J., Gao, F., & Xie, J. (2021) · Immunity Inflammation and Disease · doi:10.1002/iid3.417 · Cited by 20 · see citing works

A20 Inhibits LPS-Induced Inflammation by Regulating TRAF6 Polyubiquitination in Rainbow Trout

Jang, J. H., Kim, H. J., Jung, I. Y., & Cho, J. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189801 · Cited by 19 · see citing works

MAP3K7 and GSTZ1 are associated with human longevity: a two-stage case–control study using a multilocus genotyping

Cianni, F. D., Campa, D., Tallaro, F., Rizzato, C., Rango, F. D., Barale, R., Passarino, G., Canzian, F., Gemignani, F., Montesanto, A., et al. (2012) · AGE · doi:10.1007/s11357-012-9416-8 · Cited by 18 · see citing works

Labdanolic acid methyl ester (LAME) exerts anti-inflammatory effects through inhibition of TAK-1 activation

Cuadrado, I., Cidre‐Aranaz, F., Herránz, S., Estévez‐Braun, A., Heras, B. D. L., & Hortelano, S. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2011.10.013 · Cited by 17 · see citing works

The Biology of A20-Like Molecules

Enesa, K., & Evans, P. C. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0398-6_3 · Cited by 17 · see citing works

Endotoxin tolerance in mast cells, its consequences for IgE-mediated signalling, and the effects of BCL3 deficiency

Poplutz, M. K., Levikova, M., Lüscher‐Firzlaff, J., Lesina, M., Algül, H., Lüscher, B., & Huber, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-04890-4 · Cited by 17 · see citing works

MEK-mediated CHPF2 phosphorylation promotes colorectal cancer cell proliferation and metastasis by activating NF-κB signaling

Wen, X., Qin, J., Zhang, X., Ye, L., Wang, Y., Yang, R., Di, Y., He, W., & Wang, Z. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216644 · Cited by 16 · see citing works

An F-box protein, FBXW5, negatively regulates TAK1 MAP3K in the IL-1β signaling pathway

Minoda, Y., Sakurai, H., Kobayashi, T., Yoshimura, A., & Takaesu, G. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.02.052 · Cited by 16 · see citing works

Inhibition of Inflammatory Responses by <i>Centella asiatica</i> via Suppression of IRAK1-TAK1 in Mouse Macrophages

Cho, Y.-C., Vuong, H. L., Ha, J., Lee, S., Park, J., Wibow, A. E., & Cho, S. (2020) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x20500548 · Cited by 15 · see citing works

Sirtuin 7 Inhibitor Attenuates Colonic Mucosal Immune Activation in Mice—Potential Therapeutic Target in Inflammatory Bowel Disease

Kim, S. H., Byun, J., Jung, S., Kim, B., Lee, K., Jeon, H., Lee, J., Choi, H. S., Kim, E. S., Jeen, Y., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10112693 · Cited by 15 · see citing works

A Moderate Blast Exposure Results in Dysregulated Gene Network Activity Related to Cell Death, Survival, Structure, and Metabolism

Edwards, K. A., Motamedi, V., Osier, N. D., Kim, H., Yun, S., Cho, Y., Lai, C., Dell, K. C., Carr, W. S., Walker, P., et al. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00091 · Cited by 15 · see citing works

TAK1 (MAP3K7) Signaling Regulates Hematopoietic Stem Cells through TNF-Dependent and -Independent Mechanisms

Takaesu, G., Inagaki, M., Takubo, K., Mishina, Y. M., Hess, P. R., Dean, G. A., Yoshimura, A., Matsumoto, K., Suda, T., & Ninomiya‐Tsuji, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051073 · Cited by 14 · see citing works

TAK1 Inhibitor Enhances the Therapeutic Treatment for Glioblastoma

Campolo, M., Lanza, M., Casili, G., Paterniti, I., Filippone, A., Caffo, M., Cardali, S. M., Puliafito, I., Colarossi, C., Raciti, G., et al. (2020) · Cancers · doi:10.3390/cancers13010041 · Cited by 14 · see citing works

DUSP8/TAK1 signaling mediates neuropathic pain through regulating neuroinflammation and neuron death in a spinal nerve ligation (SNL) rat model

Liao, C., Zhou, H., Chen, H., Guo, C., Li, S., Ma, F., Yang, X., Xie, B., & Zhang, W. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109284 · Cited by 13 · see citing works

1,3,5-Trihydroxy-4-prenylxanthone represses lipopolysaccharide-induced iNOS expression via impeding posttranslational modification of IRAK-1

Chiou, W., Chen, C., Lin, I.-H., Chiu, J., & Chen, Y. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.12.022 · Cited by 12 · see citing works

PRKX down-regulates TAK1/IRF7 signaling in the antiviral innate immunity of black carp Mylopharyngodon piceus

Yang, X. Y., Ai, Y., Chen, L., Wang, C., Liu, J., Zhang, J., Li, J., Wu, H. M., Xiao, J., Chang, M., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.999219 · Cited by 12 · see citing works

Partners in crime: POPX2 phosphatase and its interacting proteins in cancer

Kim, P. R., Zhang, S., Rahmat, M. B. B., & Koh, C.-G. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03061-0 · Cited by 10 · see citing works

Ubc13 haploinsufficiency protects against age-related insulin resistance and high-fat diet-induced obesity

Joo, E., Fukushima, T., Harada, N., Reed, J. C., Matsuzawa, S.-I., & Inagaki, N. (2016) · Scientific Reports · doi:10.1038/srep35983 · Cited by 9 · see citing works

USP13 ameliorates nonalcoholic fatty liver disease through inhibiting the activation of TAK1

Tang, M. M., Cao, H., Ma, Y., Yao, S., Wei, X., Tan, Y., liu, F., Peng, Y., & Fan, N. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05465-4 · Cited by 8 · see citing works

The Emerging Role of OTUB2 in Diseases: From Cell Signaling Pathway to Physiological Function

Li, J., Zhang, N., Li, M., Hong, T., Meng, W., & Ouyang, T. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.820781 · Cited by 7 · see citing works

Synergistic action of 5Z-7-oxozeaenol and bortezomib in inducing apoptosis of Burkitt lymphoma cell line Daudi

Zhang, J., Li, B., Wu, H., Ou, J., Wei, R., Liu, J., Cai, W., Liu, X., Zhao, S., Yang, J., et al. (2015) · Tumor Biology · doi:10.1007/s13277-015-3832-1 · Cited by 7 · see citing works

Ubiquitin-mediated activation of TAK1 and IKK

Adhikari, A., Xu, M., & Chen, Z. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210413 · Cited by 455 · see citing works

Ubiquitination in signaling to and activation of IKK

Chen, Z. J. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01108.x · Cited by 419 · see citing works

Direct activation of protein kinases by unanchored polyubiquitin chains

Xia, Z.-P., Sun, L., Chen, X., Pineda, G., Jiang, X., Adhikari, A., Zeng, W., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature08247 · Cited by 570 · see citing works

Direct Activation of Protein Kinases by Ubiquitin

Baker, R., & Ghosh, S. (2009) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjp029 · Cited by 8 · see citing works

TAK1 Lys-158 but not Lys-209 is required for IL-1β-induced Lys63-linked TAK1 polyubiquitination and IKK/NF-κB activation

Fan, Y., Yu, Y., Mao, R., Zhang, H., & Yang, J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.11.017 · Cited by 50 · see citing works