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

A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840

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

Shared Principles in NF-κB Signaling

Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,494

Signaling to NF-κB

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

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

A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125

The metabolic signature of macrophage responses

Viola, A., Munari, F., Sánchez-Rodríguez, R., Scolaro, T., & Castegna, A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01462 · Cited by 2,021

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

Ubiquitin signalling in the NF-κB pathway

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

Nuclear factor-?B: its role in health and disease

Kumar, A., Takada, Y., Boriek, A., & Aggarwal, B. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0555-y · Cited by 933

Mutation of the Angelman Ubiquitin Ligase in Mice Causes Increased Cytoplasmic p53 and Deficits of Contextual Learning and Long-Term Potentiation

Jiang, Y.-H., Armstrong, D., Albrecht, U., Atkins, C. M., Noebels, J. L., Eichele, G., Sweatt, J. D., & Beaudet, A. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)80596-6 · Cited by 852

β-Amyloid Stimulation of Microglia and Monocytes Results in TNFα-Dependent Expression of Inducible Nitric Oxide Synthase and Neuronal Apoptosis

Combs, C. K., Karlo, J. C., Kao, S.-C., & Landreth, G. E. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01179.2001 · Cited by 721

A common human skin tumour is caused by activating mutations in β-catenin

Chan, E., Gat, U., McNiff, J. M., & Fuchs, E. (1999) · Nature Genetics · doi:10.1038/7747 · Cited by 612

When NRF2 Talks, Who's Listening?

Wakabayashi, N., Slocum, S. L., Skoko, J. J., Shin, S., & Kensler, T. W. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3216 · Cited by 595

CD14 and Toll-Like Receptors 2 and 4 Are Required for Fibrillar Aβ-Stimulated Microglial Activation

Reed-Geaghan, E. G., Savage, J. C., Hise, A. G., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3158-09.2009 · Cited by 591

The IκB kinase complex in NF‐κB regulation and beyond

Hinz, M., & Scheidereit, C. (2014) · The EMBO Reports · doi:10.1002/embr.201337983 · Cited by 572

Activation of the nuclear factor-kappaB by Rho, CDC42, and Rac-1 proteins

Perona, R., Montaner, S., Saniger, L., Sánchez-Pérez, I., Bravo, R., & Lacal, J. C. (1997) · Genes & Development · doi:10.1101/gad.11.4.463 · Cited by 519

Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins

Iwai, K., Drake, S. K., Wehr, N. B., Weissman, A. M., LaVaute, T., Minato, N., Klausner, R. D., Levine, R. L., & Rouault, T. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4924 · Cited by 293

A Role of Poly (ADP-Ribose) Polymerase in NF- B Transcriptional Activation

Hassa, P. O., & Hottiger, M. O. (1999) · Biological Chemistry · doi:10.1515/bc.1999.118 · Cited by 296

Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein

Webster, J. C., Jewell, C. M., Bodwell, J. E., Munck, A., Sar, M., & Cidlowski, J. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9287 · Cited by 261

Regulation of NF-κB by ubiquitination

Chen, J., & Chen, Z. J. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2012.12.005 · Cited by 258

Ultraviolet Radiation-induced Ubiquitination and Proteasomal Degradation of the Large Subunit of RNA Polymerase II

Ratner, J. N., Balasubramanian, B., Corden, J., Warren, S. L., & Bregman, D. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5184 · Cited by 233

Distinct roles for the NF-κB1 (p50) and c-Rel transcription factors in inflammatory arthritis

Campbell, I. K., Gerondakis, S., O’Donnell, K., & Wicks, I. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8298 · Cited by 168

Epstein–Barr virus-transforming protein latent infection membrane protein 1 activates transcription factor NF-κB through a pathway that includes the NF-κB-inducing kinase and the IκB kinases IKKα and IKKβ

Sylla, B. S., Hung, S. C., Davidson, D. M., Hatzivassiliou, E., Malinin, N. L., Wallach, D., Gilmore, T. D., Kieff, E., & Mosialos, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10106 · Cited by 137

A pervasive role of ubiquitin conjugation in activation and termination of IκB kinase pathways

Krappmann, D., & Scheidereit, C. (2005) · The EMBO Reports · doi:10.1038/sj.embor.7400380 · Cited by 128

Priming and Extending: A UbcH5/Cdc34 E2 Handoff Mechanism for Polyubiquitination on a SCF Substrate

Wu, K., Kovacev, J., & Pan, Z.-Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.025 · Cited by 126

A Constitutive Active MEK → ERK Pathway Negatively Regulates NF-κB-dependent Gene Expression by Modulating TATA-binding Protein Phosphorylation

Carter, A. B., & Hunninghake, G. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003599200 · Cited by 119

Ubiquitin, TAK1 and IKK: is there a connection?

Chen, Z. J., Bhoj, V, & Seth, R. B. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401869 · Cited by 115

Linear ubiquitination at a glance

Spit, M., Rieser, E., & Walczak, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.208512 · Cited by 94

Serum amyloid A1 mediates myotube atrophy via Toll‐like receptors

Hahn, A., Kny, M., Pablo‐Tortola, C., Todiras, M., Willenbrock, M., Schmidt, S., Schmoeckel, K., Jorde, I., Nowak, M., Jarosch, E., et al. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12491 · Cited by 67

Proapoptotic regimes for HTLV-I-transformed cells: targeting Tax and the NF-κB pathway

Kfoury, Y., Nasr, R., Hermine, O., de Thé, H., & Bazarbachi, A. (2005) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401624 · Cited by 40

Cullin 3, a cellular scripter of the non-proteolytic ubiquitin code

Jerabkova, K., & Sumara, I. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.12.007 · Cited by 33

Captopril-impaired production of tumor necrosis factor-α–induced interleukin-1β in human monocytes is associated with altered intracellular distribution of nuclear factor-κB

Andersson, P. (2002) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(02)00024-0 · Cited by 20