TAB2 and TAB3 Activate the NF-κB Pathway through Binding to Polyubiquitin Chains

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

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

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways

Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., & Khochbin, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8035-8044.2001 · Cited by 335

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221

Ubiquitin signalling in the NF-κB pathway

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

Role of Pro-Inflammatory Cytokines Released from Microglia in Neurodegenerative Diseases

Smith, J. A., Das, A., Ray, S. K., & Banik, N. L. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.10.004 · Cited by 1,165

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

Interleukin-1 (IL-1) Pathway

Weber, A., Wasiliew, P., & Kracht, M. (2010) · Science Signaling · doi:10.1126/scisignal.3105cm1 · Cited by 962

The emerging complexity of protein ubiquitination

Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821

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

Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages

Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 619

Osteoimmunology: The conceptual framework unifying the immune and skeletal systems

Okamoto, K., Nakashima, T., Shinohara, M., Negishi-Koga, T., Komatsu, N., Terashima, A., Sawa, S., Nitta, T., & Takayanagi, H. (2017) · Physiological Reviews · doi:10.1152/physrev.00036.2016 · Cited by 534

NF-κB-Independent Role of IKKα/IKKβ in Preventing RIPK1 Kinase-Dependent Apoptotic and Necroptotic Cell Death during TNF Signaling

Dondelinger, Y., Jouan-Lanhouet, S., Divert, T., Theatre, E., Bertin, J., Gough, P. J., Giansanti, P., Heck, A. J. R., Dejardin, E., Vandenabeele, P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.032 · Cited by 431

The microRNA miR-23b suppresses IL-17-associated autoimmune inflammation by targeting TAB2, TAB3 and IKK-α

Zhu, S., Pan, W., Song, X., Liu, Y., Shao, X., Tang, Y., Liang, D., He, D., Wang, H., Liu, W., et al. (2012) · Nature Medicine · doi:10.1038/nm.2815 · Cited by 396

Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis

Geng, J., Ito, Y., Shi, L., Amin, P., Chu, J., Ouchida, A. T., Mookhtiar, A. K., Zhao, H., Xu, D., Shan, B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00406-w · Cited by 325

Principles of Ubiquitin-Dependent Signaling

Oh, E., Akopian, D., & Rape, M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062802 · Cited by 339

Novel cross-talk within the IKK family controls innate immunity

Clark, K., Peggie, M., Plater, L., Sorcek, R. J., Young, E. R. R., Madwed, J. B., Hough, J., McIver, E. G., & Cohen, P. (2011) · Biochemical Journal · doi:10.1042/bj20101701 · Cited by 326

Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms

de Bie, P., & Ciechanover, A. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.16 · Cited by 296

TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation

Lafont, E., Draber, P., Rieser, E., Reichert, M., Kupka, S., de Miguel, D., Draberova, H., von Mässenhausen, A., Bhamra, A., Henderson, S., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0229-6 · Cited by 283

A Cytoplasmic ATM-TRAF6-cIAP1 Module Links Nuclear DNA Damage Signaling to Ubiquitin-Mediated NF-κB Activation

Hinz, M., Stilmann, M., Arslan, S. Ç., Khanna, K. K., Dittmar, G., & Scheidereit, C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.008 · Cited by 280

Ubiquitination of RIP Is Required for Tumor Necrosis Factor α-induced NF-κB Activation

Li, H., Kobayashi, M., Blonska, M., You, Y., & Lin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600620200 · Cited by 277

Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake

Gong, Y., Lee, J. N., Lee, P. C. W., Goldstein, J. L., Brown, M. S., & Ye, J. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2005.11.014 · Cited by 262

Ubiquitin in the immune system

Zinngrebe, J., Montinaro, A., Peltzer, N., & Walczak, H. (2014) · The EMBO Reports · doi:10.1002/embr.201338025 · Cited by 227

Negative regulation of IL-17-mediated signaling and inflammation by the ubiquitin-specific protease USP25

Zhong, B., Liu, X., Wang, X., Chang, S. H., Liu, X., Wang, A., Reynolds, J. M., & Dong, C. (2012) · Nature Immunology · doi:10.1038/ni.2427 · Cited by 206

Linear Ubiquitin Assembly Complex Negatively Regulates RIG-I- and TRIM25-Mediated Type I Interferon Induction

Inn, K.-S., Gack, M. U., Tokunaga, F., Shi, M., Wong, L.-Y., Iwai, K., & Jung, J. U. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.029 · Cited by 209

Poly-ubiquitination in TNFR1-mediated necroptosis

Dondelinger, Y., Darding, M., Bertrand, M. J. M., & Walczak, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2191-4 · Cited by 173

TRAF6 ubiquitin ligase is essential for RANKL signaling and osteoclast differentiation

Lamothe, B., Webster, W. K., Gopinathan, A., Besse, A., Campos, A. D., & Darnay, B. G. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.017 · Cited by 134

K63-polyubiquitinated HAUSP deubiquitinates HIF-1α and dictates H3K56 acetylation promoting hypoxia-induced tumour progression

Wu, H.-T., Kuo, Y.-C., Hung, J.-J., Huang, C.-H., Chen, W.-Y., Chou, T.-Y., Chen, Y., Chen, Y.-J., Chen, Y.-J., Cheng, W.-C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13644 · Cited by 129

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

Linear ubiquitination at a glance

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

miR-155 Regulates Immune Modulatory Properties of Mesenchymal Stem Cells by Targeting TAK1-binding Protein 2

Xu, C., Ren, G., Cao, G., Chen, Q., Shou, P., Zheng, C., Du, L., Han, X., Jiang, M., Yang, Q., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.414862 · Cited by 84

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

Exercise Training Modulates Adipokine Dysregulations in Metabolic Syndrome

Babaei, P., & Hoseini, R. (2022) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2022.01.001 · Cited by 52

TAB2 Scaffolds TAK1 and NLK in Repressing Canonical Wnt Signaling

Li, M., Wang, H., Huang, T., Wang, J., Ding, Y., Li, Z., Zhang, J., & Li, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083246 · Cited by 32

The API2–MALT1 fusion exploits TNFR pathway-associated RIP1 ubiquitination to promote oncogenic NF-κB signaling

Rosebeck, S., Rehman, A. O., Apel, I. J., Kohrt, D., Appert, A., O'Donnell, M. A., Ting, A. T., Du, M.-Q., Baens, M., Lucas, P. C., et al. (2014) · Oncogene · doi:10.1038/onc.2013.195 · Cited by 27