Ubiquitin in the immune system

Dendritic cells and the control of immunity

Banchereau, J., & Steinman, R. M. (1998) · Nature · doi:10.1038/32588 · Cited by 14,486

Pathogen Recognition and Innate Immunity

Akira, S., Uematsu, S., & Takeuchi, O. (2006) · Cell · doi:10.1016/j.cell.2006.02.015 · Cited by 12,401

Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls

The Wellcome Trust Case Control Consortium, Management Committee, Burton, P. R., Clayton, D. G., Cardon, L. R., Craddock, N., Deloukas, P., Duncanson, A., Kwiatkowski, D. P., McCarthy, M. I., et al. (2007) · Nature · doi:10.1038/nature05911 · Cited by 9,442

Pattern Recognition Receptors and Inflammation

Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895

Innate immune recognition

Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394

An endotoxin-induced serum factor that causes necrosis of tumors

Carswell, E. A., Old, L. J., Kassel, R. L., Green, S., Fiore, N., & Williamson, B. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3666 · Cited by 4,532

The Danger Model: A Renewed Sense of Self

Matzinger, P. (2002) · Science · doi:10.1126/science.1071059 · Cited by 4,205

Approaching the asymptote? Evolution and revolution in immunology.Preprint

Janeway, C. (1989) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1989.054.01.003 · Cited by 3,396

Activation and regulation of the inflammasomes

Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884

Recognition of microorganisms and activation of the immune response

Medzhitov, R. (2007) · Nature · doi:10.1038/nature06246 · Cited by 2,862

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

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

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679

Projection of an Immunological Self Shadow Within the Thymus by the Aire Protein

Anderson, M. S., Venanzi, E. S., Klein, L., Chen, Z.-B., Berzins, S., Turley, S., von Boehmer, H., Bronson, R., Dierich, A., Benoist, C., et al. (2002) · Science · doi:10.1126/science.1075958 · Cited by 2,582

Shock and Tissue Injury Induced by Recombinant Human Cachectin

Tracey, K. J., Beutler, B., Lowry, S. F., Merryweather, J., Wolpe, S., Milsark, I. W., Hariri, R. J., Fahey, T. J., Zentella, A., Albert, J. D., et al. (1986) · Science · doi:10.1126/science.3764421 · Cited by 2,549

ROLE OF CYTOKINES IN RHEUMATOID ARTHRITIS

Feldmann, M., Brennan, F. M., & Maini, R. N. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.397 · Cited by 2,507

Molecular mechanisms of necroptosis: an ordered cellular explosion

Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382

Passive Immunization Against Cachectin/Tumor Necrosis Factor Protects Mice from Lethal Effect of Endotoxin

Beutler, B., Milsark, I. W., & Cerami, A. (1985) · Science · doi:10.1126/science.3895437 · Cited by 2,344

Proteomic analysis of post-translational modifications

Mann, M., & Jensen, O. N. (2003) · Nature Biotechnology · doi:10.1038/nbt0303-255 · Cited by 2,176

The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation

Hsu, H., Xiong, J., & Goeddel, D. V. (1995) · Cell · doi:10.1016/0092-8674(95)90070-5 · Cited by 2,024

TRADD–TRAF2 and TRADD–FADD Interactions Define Two Distinct TNF Receptor 1 Signal Transduction Pathways

Hsu, H., Shu, H., Pan, M., & Goeddel, D. V. (1996) · Cell · doi:10.1016/s0092-8674(00)80984-8 · Cited by 1,998

Breaking the chains: structure and function of the deubiquitinases

Komander, D., Clague, M. J., & Urbé, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2731 · Cited by 1,969

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 1,889

Nod2-Dependent Regulation of Innate and Adaptive Immunity in the Intestinal Tract

Kobayashi, K. S., Chamaillard, M., Ogura, Y., Henegariu, O., Inohara, N., Núñez, G., & Flavell, R. A. (2005) · Science · doi:10.1126/science.1104911 · Cited by 1,834

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

Signaling in innate immunity and inflammation

Newton, K., & Dixit, V. M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006049 · Cited by 1,513

T cell anergy

Schwartz, R. H. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141110 · Cited by 1,487

Failure to Regulate TNF-Induced NF-κB and Cell Death Responses in A20-Deficient Mice

Lee, E. G., Boone, D. L., Chai, S., Libby, S. L., Chien, M., Lodolce, J. P., & Ma, A. (2000) · Science · doi:10.1126/science.289.5488.2350 · Cited by 1,409

Germline Mutations in the Extracellular Domains of the 55 kDa TNF Receptor, TNFR1, Define a Family of Dominantly Inherited Autoinflammatory Syndromes

McDermott, M., Aksentijevich, I. A., Galon, J., McDermott, E. M., Ogunkolade, B.-W., Centola, M. B., Mansfield, E. A., Gadina, M., Karenko, L., Pettersson, T., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80721-7 · Cited by 1,404

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 1,398

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 1,253

An autoimmune disease, APECED, caused by mutations in a novel gene featuring two PHD-type zinc-finger domains

Aaltonen, J., Björses, P., Perheentupa, J., Horelli‐Kuitunen, N., Palotie, A. V., Peltonen, L., Lee, Y. S., Francis, F., Henning, S., Thiel, C. S., et al. (1997) · Nature Genetics · doi:10.1038/ng1297-399 · Cited by 1,214

TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex

Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182

Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.

Hershko, A., Heller, H., Elias, S., & Ciechanover, A. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82050-x · Cited by 1,160

Physiological functions of the HECT family of ubiquitin ligases

Rotin, D., & Kumar, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2690 · Cited by 1,105

The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses

Boone, D. L., Turer, E. E., Lee, E. G., Ahmad, R., Wheeler, M. T., Tsui, C., Hurley, P. J., Chien, M., Chai, S., Hitotsumatsu, O., et al. (2004) · Nature Immunology · doi:10.1038/ni1110 · Cited by 1,104

Activation of IKK by TNFα Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO

Ea, C.-K., Deng, L., Xia, Z.-P., Pineda, G., & Chen, Z. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.026 · Cited by 1,026

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

Building ubiquitin chains: E2 enzymes at work

Ye, Y., & Rape, M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2780 · Cited by 989

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

Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6

Häcker, H., Redecke, V., Blagoev, B., Kratchmarova, I., Hsu, L.-C., Wang, G. G., Kamps, M. P., Raz, E., Wagner, H., Häcker, G. A., et al. (2005) · Nature · doi:10.1038/nature04369 · Cited by 962

Involvement of linear polyubiquitylation of NEMO in NF-κB activation

Tokunaga, F., Sakata, S., Saeki, Y., Satomi, Y., Kirisako, T., Kamei, K., Nakagawa, T., Kato, M., Murata, S., Yamaoka, S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1821 · Cited by 960

Toll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKL

Kaiser, W. J., Sridharan, H., Huang, C., Mandal, P., Upton, J. W., Gough, P. J., Sehon, C. A., Marquis, R. W., Bertin, J., & Mocarski, E. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462341 · Cited by 959

Nonproteolytic Functions of Ubiquitin in Cell Signaling

Chen, Z. J., & Sun, L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.014 · Cited by 948

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

Linear ubiquitination prevents inflammation and regulates immune signalling

Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940

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

Kanayama, A., Seth, R. B., Sun, L., Ea, C.-K., Hong, M., Shaito, A. A., Chiu, Y., Deng, L., & Chen, Z. J. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.008 · Cited by 911

Ubiquitin-binding domains — from structures to functions

Đikić, I., Wakatsuki, S., & Walters, K. J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2767 · Cited by 903

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 878

Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey

Aggarwal, B. B., Gupta, S. C., & Kim, J. H. (2012) · Blood · doi:10.1182/blood-2011-04-325225 · Cited by 877

A ubiquitin ligase complex assembles linear polyubiquitin chains

Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., & Iwaï, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601360 · Cited by 803

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 797

Ubiquitin-binding domains

Hicke, L., Schubert, H., & Hill, C. P. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1701 · Cited by 795

Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation

Rahighi, S., Ikeda, F., Kawasaki, M., Akutsu, M., Suzuki, N., Kato, R., Kensche, T., Uejima, T., Bloor, S., Komander, D., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.007 · Cited by 761

Control of B-cell responses by Toll-like receptors

Pasare, C., & Medzhitov, R. M. (2005) · Nature · doi:10.1038/nature04267 · Cited by 752

SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis

Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745

Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity

Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718

Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b

Bachmaier, K., Krawczyk, C. M., Kozieradzki, I., Kong, Y., Sasaki, T., Oliveira-dos-Santos, A., Mariathasan, S., Bouchard, D., Wakeham, A. C., Itié, A., et al. (2000) · Nature · doi:10.1038/35003228 · Cited by 674

NLRs join TLRs as innate sensors of pathogens

Martinon, F., & Tschopp, J. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.06.004 · Cited by 673

Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death

Ofengeim, D., & Yuan, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3683 · Cited by 635

Ubiquitylation in innate and adaptive immunity

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

Cbl: many adaptations to regulate protein tyrosine kinases

Thien, C. B. F., & Langdon, W. Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35067100 · Cited by 628

Cbl-b regulates the CD28 dependence of T-cell activation

Chiang, Y. J., Kole, H. K., Brown, K. E., Naramura, M., Fukuhara, S., Hu, R.-J., Jang, I. K., Gutkind, J. S., Shevach, E. M., & Gu, H. (2000) · Nature · doi:10.1038/35003235 · Cited by 626

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

Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation

Wu, C.-J., Conze, D. B., Li, T., Srinivasula, S. M., & Ashwell, J. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1384 · Cited by 619

Ubiquitin-binding domains

Hurley, J. H., Lee, S., & Prag, G. (2006) · Biochemical Journal · doi:10.1042/bj20061138 · Cited by 614

The enemy within: keeping self-reactive T cells at bay in the periphery

Walker, L. S. K., & Abbas, A. K. (2002) · Nature reviews. Immunology · doi:10.1038/nri701 · Cited by 612

SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex

Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S.-I., Tanaka, K., Nakano, H., & Iwai, K. (2011) · Nature · doi:10.1038/nature09815 · Cited by 609

Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains

Komander, D., Reyes‐Turcu, F. E., Licchesi, J. D. F., Odenwälder, P., Wilkinson, K. D., & Barford, D. (2009) · EMBO Reports · doi:10.1038/embor.2009.55 · Cited by 575

Promiscuous gene expression in thymic epithelial cells is regulated at multiple levels

Derbinski, J., Gäbler, J., Brors, B., Tierling, S., Jonnakuty, S., Hergenhahn, M., Peltonen, L., Walter, J., & Kyewski, B. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050471 · Cited by 564

Structure of an E6AP-UbcH7 Complex: Insights into Ubiquitination by the E2-E3 Enzyme Cascade

Huang, L., Kinnucan, E., Wang, G., Beaudenon, S. L., Howley, P. M., Huibregtse, J. M., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.286.5443.1321 · Cited by 562

UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids

Wenzel, D. M., Lissounov, A., Brzović, P. S., & Klevit, R. E. (2011) · Nature · doi:10.1038/nature09966 · Cited by 560

Two independent alleles at 6q23 associated with risk of rheumatoid arthritis

Plenge, R. M., Cotsapas, C. J., Davies, L. R. L., Price, A. L., de Bakker, P. I. W., Maller, J., Pe’er, I., Burtt, N. P., Blumenstiel, B. S., DeFelice, M., et al. (2007) · Nature Genetics · doi:10.1038/ng.2007.27 · Cited by 552

Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins

Heissmeyer, V., Macián, F., Im, S., Varma, R., Feske, S., Venuprasad, K., Gu, H., Liu, Y., Dustin, M. L., & Rao, A. (2004) · Nature Immunology · doi:10.1038/ni1047 · Cited by 515

OTULIN Antagonizes LUBAC Signaling by Specifically Hydrolyzing Met1-Linked Polyubiquitin

Keusekotten, K., Elliott, P. R., Glockner, L., Fiil, B. K., Damgaard, R. B., Kulathu, Y., Wauer, T., Hospenthal, M. K., Gyrd‐Hansen, M., Krappmann, D., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.014 · Cited by 508

The Tumor Necrosis Factor Family Receptors RANK and CD40 Cooperatively Establish the Thymic Medullary Microenvironment and Self-Tolerance

Akiyama, T., Shimo, Y., Yanai, H., Qin, J., Ohshima, D., Maruyama, Y., Asaumi, Y., Kitazawa, J., Takayanagi, H., Penninger, J. M., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.06.015 · Cited by 503

Caspase 8 inhibits programmed necrosis by processing CYLD

O’Donnell, M. A., Perez-Jimenez, E., Oberst, A., Ng, A., Massoumi, R., Xavier, R., Green, D. R., & Ting, A. T. (2011) · Nature Cell Biology · doi:10.1038/ncb2362 · Cited by 494

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

The ubiquitin-editing enzyme A20 (TNFAIP3) is a central regulator of immunopathology

Vereecke, L., Beyaert, R., & Loo, G. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.05.007 · Cited by 490

Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency

Boisson, B., Laplantine, E., Prando, C., Giliani, S., Israelsson, E., Xu, Z., Abhyankar, A., Israël, L., Trevejo-Nuñez, G., Bogunovic, D., et al. (2012) · Nature Immunology · doi:10.1038/ni.2457 · Cited by 489

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 483

Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125

Arimoto, K., Takahashi, H., Hishiki, T., Konishi, H., Fujita, T., & Shimotohno, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611551104 · Cited by 482

Multiple polymorphisms in the TNFAIP3 region are independently associated with systemic lupus erythematosus

Musone, S. L., Taylor, K. E., Lu, T. T., Nititham, J., Ferreira, R. C., Ortmann, W. A., Shifrin, N. T., Petri, M., Kamboh, M. I., Manzi, S., et al. (2008) · Nature Genetics · doi:10.1038/ng.202 · Cited by 470

Aire deficient mice develop multiple features of APECED phenotype and show altered immune response

Ramsey, C. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.4.397 · Cited by 466

A Deubiquitinase That Regulates Type I Interferon Production

Kayagaki, N., Phung, Q. T., Chan, S. B., Chaudhari, R., Quan, C., O’Rourke, K. M., Eby, M. T., Pietras, E. M., Cheng, G., Bazán, J. F., et al. (2007) · Science · doi:10.1126/science.1145918 · Cited by 452

Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains

Emmerich, C. H., Ordureau, A., Strickson, S., Arthur, J. S. C., Pedrioli, P. G. A., Komander, D., & Cohen, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314715110 · Cited by 442

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

Infectious Diseases in Patients with IRAK-4, MyD88, NEMO, or IκBα Deficiency

Pïcard, C., Casanova, J., & Puel, A. (2011) · Clinical Microbiology Reviews · doi:10.1128/cmr.00001-11 · Cited by 408

Ubiquitin-Induced Oligomerization of the RNA Sensors RIG-I and MDA5 Activates Antiviral Innate Immune Response

Jiang, X., Kinch, L. N., Brautigam, C. A., Chen, X., Du, F., Grishin, N. V., & Chen, Z. J. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.022 · Cited by 407

Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines

Tseng, P., Matsuzawa, A., Zhang, W., Mino, T., Vignali, D. A. A., & Karin, M. (2009) · Nature Immunology · doi:10.1038/ni.1819 · Cited by 403

The Ubiquitin Ligase XIAP Recruits LUBAC for NOD2 Signaling in Inflammation and Innate Immunity

Damgaard, R. B., Nachbur, U., Yabal, M., Wong, W. W.-L., Fiil, B. K., Kastirr, M., Rieser, E., Rickard, J. A., Bankovacki, A., Peschel, C., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.014 · Cited by 396

Anti-TNF biologic agents: still the therapy of choice for rheumatoid arthritis

Taylor, P., & Feldmann, M. (2009) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2009.181 · Cited by 391

Toll-Dependent Control Mechanisms of CD4 T Cell Activation

Pasare, C., & Medzhitov, R. M. (2004) · Immunity · doi:10.1016/j.immuni.2004.10.006 · Cited by 383

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 369

The Ubiquitin-Editing Enzyme A20 Restricts Nucleotide-Binding Oligomerization Domain Containing 2-Triggered Signals

Hitotsumatsu, O., Ahmad, R., Tavares, R. M., Wang, M., Philpott, D. J., Turer, E. E., Lee, B. L., Shiffin, N., Advincula, R., Malynn, B. A., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.02.002 · Cited by 357

The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice

Perry, W. L., Hustad, C., Swing, D. A., O'Sullivan, T., Jenkins, N., & Copeland, N. (1998) · Nature Genetics · doi:10.1038/ng0298-143 · Cited by 354

MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades

Liu, S., Chen, J., Cai, X., Wu, J., Chen, X., Wu, Y.-T., Sun, L., & Chen, Z. J. (2013) · eLife · doi:10.7554/elife.00785 · Cited by 354

The role of ubiquitylation in immune defence and pathogen evasion

Jiang, X., & Chen, Z. J. (2011) · Nature reviews. Immunology · doi:10.1038/nri3111 · Cited by 352

Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction

Jeon, M.-S., Atfield, A., Venuprasad, K., Krawczyk, C., Sarao, R., Elly, C., Yang, C., Arya, S., Bachmaier, K., Su, L., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.07.013 · Cited by 348

Cellular Inhibitors of Apoptosis cIAP1 and cIAP2 Are Required for Innate Immunity Signaling by the Pattern Recognition Receptors NOD1 and NOD2

Bertrand, M. J. M., Doiron, K., Labbè, K., Korneluk, R. G., Barker, P. A., & Saleh, M. (2009) · Immunity · doi:10.1016/j.immuni.2009.04.011 · Cited by 347

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

PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4

You, F., Sun, H., Zhou, X., Sun, W., Liang, S., Zhai, Z., & Jiang, Z. (2009) · Nature Immunology · doi:10.1038/ni.1815 · Cited by 340

The tumour suppressor CYLD is a negative regulator of RIG‐I‐mediated antiviral response

Friedman, C. S., O’Donnell, M. A., Legarda, D., Ng, A., Cardenas, W. B., Yount, J. S., Moran, T. M., Basler, C. F., Komuro, A., Horvath, C. M., et al. (2008) · EMBO Reports · doi:10.1038/embor.2008.136 · Cited by 334

Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne

Bremm, A., Freund, S. M. V., & Komander, D. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1873 · Cited by 332

A tagging-via-substrate technology for detection and proteomics of farnesylated proteins

Kho, Y., Kim, S. C., Chen, J., Barma, D. K., Kwon, S. W., Cheng, J., Jaunbergs, J., Weinbaum, C., Tamanoi, F., Falck, J. R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403413101 · Cited by 328

"Covalent affinity" purification of ubiquitin-activating enzyme.

Ciechanover, A. J., Elias, S., Heller, H., & Hershko, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34957-3 · Cited by 320

The BRCA1/BARD1 Heterodimer Assembles Polyubiquitin Chains through an Unconventional Linkage Involving Lysine Residue K6 of Ubiquitin

Wu-Baer, F., Lagrazon, K., Yuan, W., & Baer, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300249200 · Cited by 311

A20: Central Gatekeeper in Inflammation and Immunity

Coornaert, B., Carpentier, I., & Beyaert, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800032200 · Cited by 309

TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway

Michallet, M., Meylan, E., Ermolaeva, M., Vázquez, J., Rebsamen, M., Curran, J. A., Poeck, H., Bscheider, M., Hartmann, G., König, M. F., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.03.013 · Cited by 304

Development of Autoimmunity against Transcriptionally Unrepressed Target Antigen in the Thymus of Aire-Deficient Mice

Kuroda, N., Mitani, T., Takeda, N., Ishimaru, N., Arakaki, R., Hayashi, Y., Bando, Y., Izumi, K., Takahashi, T., Nomura, T., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.4.1862 · Cited by 299

A20 (TNFAIP3) deficiency in myeloid cells triggers erosive polyarthritis resembling rheumatoid arthritis

Matmati, M., Jacques, P., Maelfait, J., Verheugen, E., Kool, M., Sze, M., Geboes, L., Louagie, E., Guire, C. M., Vereecke, L., et al. (2011) · Nature Genetics · doi:10.1038/ng.874 · Cited by 294

The treatment of malignant tumors by bacterial toxins as developed by the late William B. Coley, M.D., reviewed in the light of modern research.

Nauts, H. C., Swift, W. E., & Coley, B. L. (1946) · PubMed · Cited by 290

The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis

Rivkin, E., Almeida, S. M., Ceccarelli, D. F. J., Juang, Y.-C. A., MacLean, T. A., Srikumar, T., Huang, H., Dunham, W. H., Fukumura, R., ., G. X., et al. (2013) · Nature · doi:10.1038/nature12296 · Cited by 288

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

Autoimmune Regulator Is Expressed in the Cells Regulating Immune Tolerance in Thymus Medulla

Heino, M., Peterson, P., Kudoh, J., Nagamine, K., Lagerstedt, A., Ovod, V., Ranki, A., Rantala, I. S., Nieminen, M. S., Tuukkanen, J., et al. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0308 · Cited by 286

Untitled work

Anandasabapathy (2003) · doi:10.1016/s1074-7613(03)00084-0 · Cited by 285

The Mechanism of Linkage-Specific Ubiquitin Chain Elongation by a Single-Subunit E2

Wickliffe, K. E., Lorenz, S., Wemmer, D. E., Kuriyan, J., & Rapé, M. (2011) · Cell · doi:10.1016/j.cell.2011.01.035 · Cited by 282

BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair

Morris, J. R., & Solomon, E. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh095 · Cited by 282

Proteolysis-independent regulation of PI3K by Cbl-b–mediated ubiquitination in T cells

Fang, D., & Liu, Y. (2001) · Nature Immunology · doi:10.1038/ni0901-870 · Cited by 279

OTULIN Restricts Met1-Linked Ubiquitination to Control Innate Immune Signaling

Fiil, B. K., Damgaard, R. B., Wagner, S., Keusekotten, K., Fritsch, M., Bekker‐Jensen, S., Mailand, N., Choudhary, C., Komander, D., & Gyrd‐Hansen, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.004 · Cited by 275

Dependence of Self-Tolerance on TRAF6-Directed Development of Thymic Stroma

Akiyama, T., Maeda, S., Yamane, S., Ogino, K., Kasai, M., Kajiura, F., Matsumoto, M., & Inoue, J. (2005) · Science · doi:10.1126/science.1105677 · Cited by 270

Homeostatic MyD88-dependent signals cause lethal inflamMation in the absence of A20

Turer, E. E., Tavares, R. M., Mortier, E., Hitotsumatsu, O., Advincula, R., Lee, B. L., Shifrin, N. T., Malynn, B. A., & Ma, A. I. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071108 · Cited by 267

Regulation of NF‐κB by deubiquitinases

Harhaj, E. W., & Dixit, V. M. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01100.x · Cited by 266

Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production

Chang, M., Jin, W., & Sun, S. (2009) · Nature Immunology · doi:10.1038/ni.1777 · Cited by 259

The Ubiquitin-Editing Protein A20 Prevents Dendritic Cell Activation, Recognition of Apoptotic Cells, and Systemic Autoimmunity

Kool, M., Loo, G., Waelput, W., Prijck, S. D., Muskens, F., Sze, M., Praet, J. T. V., Branco‐Madeira, F., Janssens, S., Reizis, B., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.013 · Cited by 257

Structural Basis for Recognition of Diubiquitins by NEMO

Lo, Y.-C., Lin, S., Rospigliosi, C. C., Conze, D. B., Wu, C.-J., Ashwell, J. D., Eliezer, D., & Wu, H. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.012 · Cited by 257

Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses

Reiley, W. W., Jin, W., Lee, A. J., Wright, A., Wu, X., Tewalt, E. F., Leonard, T. O., Norbury, C. C., Fitzpatrick, L. R., Zhang, M., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062694 · Cited by 255

A Ubiquitin Replacement Strategy in Human Cells Reveals Distinct Mechanisms of IKK Activation by TNFα and IL-1β

Xu, M., Skaug, B. A., Zeng, W., & Chen, Z. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.002 · Cited by 248

Polyubiquitination by HECT E3s and the Determinants of Chain Type Specificity

Kim, H. C., & Huibregtse, J. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00240-09 · Cited by 247

Impaired regulation of NF-κB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice

Zhang, J., Stirling, B., Temmerman, S. T., Ma, C. A., Fuss, I. J., Derry, J. M. J., & Jain, A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28746 · Cited by 245

TRAF2 Must Bind to Cellular Inhibitors of Apoptosis for Tumor Necrosis Factor (TNF) to Efficiently Activate NF-κB and to Prevent TNF-induced Apoptosis

Vince, J. E., Pantaki-Eimany, D., Feltham, R., Mace, P. D., Cordier, S. M., Schmukle, A. C., Davidson, A. J., Callus, B. A., Wong, W. W.-L., Gentle, I. E., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.072256 · Cited by 241

Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1

Glauser, L., Sonnay, S., Stafa, K., & Moore, D. J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07318.x · Cited by 230

LUBAC synthesizes linear ubiquitin chains via a thioester intermediate

Stieglitz, B., Morris-Davies, A. C., Koliopoulos, M. G., Christodoulou, E., & Rittinger, K. (2012) · EMBO Reports · doi:10.1038/embor.2012.105 · Cited by 225

Control of AMPK-related kinases by USP9X and atypical Lys29/Lys33-linked polyubiquitin chains

Al-Hakim, A., Zagórska, A., Chapman, L., Deák, M., Peggie, M. W., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20080067 · Cited by 224

The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING‐IBR‐RING domain and the unique LDD extension

Smit, J. J., Monteferrario, D., Noordermeer, S. M., van Dijk, W. J., van der Reijden, B. A., & Sixma, T. K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.217 · Cited by 221

Essential Cytoplasmic Translocation of a Cytokine Receptor–Assembled Signaling Complex

Matsuzawa, A., Tseng, P., Vallabhapurapu, S., Luo, J., Zhang, W., Wang, H., Vignali, D. A. A., Gallagher, E. D., & Karin, M. (2008) · Science · doi:10.1126/science.1157340 · Cited by 217

Cbl-b Is a Negative Regulator of Receptor Clustering and Raft Aggregation in T Cells

Krawczyk, C. M., Bachmaier, K., Sasaki, T., Jones, R. G., Snapper, S. B., Bouchard, D., Kozieradzki, I., Ohashi, P. S., Alt, F. W., & Penninger, J. M. (2000) · Immunity · doi:10.1016/s1074-7613(00)00046-7 · Cited by 216

Negative Regulation of the Retinoic Acid-inducible Gene I-induced Antiviral State by the Ubiquitin-editing Protein A20

Lin, R., Yang, L., Nakhaei, P., Sun, Q., Sharif‐Askari, E., Julkunen, I., & Hiscott, J. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510326200 · Cited by 215

Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis

Seymour, R. E., Hasham, M. G., Cox, G. A., Shultz, L. D., HogenEsch, H., Roopenian, D. C., & Sundberg, J. P. (2007) · Genes and Immunity · doi:10.1038/sj.gene.6364403 · Cited by 212

Structural basis and specificity of human otubain 1-mediated deubiquitination

Edelmann, M. J., Iphöfer, A., Akutsu, M., Altun, M., di Gleria, K., Kramer, H., Fiebiger, E., Dhe‐Paganon, S., & Kessler, B. M. (2008) · Biochemical Journal · doi:10.1042/bj20081318 · Cited by 212

Regulation of Early Wave of Germ Cell Apoptosis and Spermatogenesis by Deubiquitinating Enzyme CYLD

Wright, A., Reiley, W. W., Chang, M., Jin, W., Lee, A. J., Zhang, M., & Sun, S. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.09.007 · Cited by 212

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

The ‘complexities’ of life and death: Death receptor signalling platforms

Dickens, L. S., Powley, I. R., Hughes, M. A., & MacFarlane, M. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.04.005 · Cited by 208

RIG-I RNA Helicase Activation of IRF3 Transcription Factor Is Negatively Regulated by Caspase-8-Mediated Cleavage of the RIP1 Protein

Rajput, A., Kovalenko, A., Bogdanov, K., Yang, S., Kang, T., Kim, J., Du, J., & Wallach, D. (2011) · Immunity · doi:10.1016/j.immuni.2010.12.018 · Cited by 203

Human ITCH E3 Ubiquitin Ligase Deficiency Causes Syndromic Multisystem Autoimmune Disease

Lohr, N. J., Molleston, J. P., Strauss, K. A., Torres‐Martinez, W., Sherman, E. A., Squires, R. H., Rider, N. L., Chikwava, K. R., Cummings, O. W., Morton, D. H., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.028 · Cited by 200

Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-κB signalling

Trynka, G., Zhernakova, A., Romanos, J., Franke, L., Hunt, K. A., Turner, G., Bruinenberg, M., Heap, G., Platteel, M., Ryan, A. W., et al. (2009) · Gut · doi:10.1136/gut.2008.169052 · Cited by 199

K11-linked ubiquitin chains as novel regulators of cell division

Wickliffe, K. E., Williamson, A. P., Meyer, H., Kelly, A., & Rapé, M. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.08.008 · Cited by 196

Mass Spectrometric and Mutational Analyses Reveal Lys-6-linked Polyubiquitin Chains Catalyzed by BRCA1-BARD1 Ubiquitin Ligase

Nishikawa, H., Ooka, S., Sato, K., Arima, K., Okamoto, J., Klevit, R. E., Fukuda, M., & Ohta, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308540200 · Cited by 194

B cells lacking the tumor suppressor TNFAIP3/A20 display impaired differentiation and hyperactivation and cause inflammation and autoimmunity in aged mice

Chu, Y., Vahl, J. C., Kumar, D., Heger, K., Bertossi, A., Wojtowicz, E. E., Soberon, V., Schenten, D., Mack, B., Reutelshöfer, M., et al. (2010) · Blood · doi:10.1182/blood-2010-09-306019 · Cited by 191

Ubiquitin Binding to A20 ZnF4 Is Required for Modulation of NF-κB Signaling

Bosanac, I., Wertz, I. E., Pan, B., Yu, C., Kusam, S., Lam, C., Phu, L., Phung, Q. T., Maurer, B., Arnott, D. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.009 · Cited by 190

Cutting Edge: Roles of Caspase-8 and Caspase-10 in Innate Immune Responses to Double-Stranded RNA

Takahashi, K., Kawai, T., Kumar, H., Sato, S., Yonehara, S., & Akira, S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4520 · Cited by 186

Dimerization and Ubiquitin Mediated Recruitment of A20, a Complex Deubiquitinating Enzyme

Lu, T. T., Onizawa, M., Hammer, G. E., Turer, E. E., Yin, Q., Damko, E., Agelidis, A. M., Shifrin, N. T., Advincula, R., Barrera, J., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.03.008 · Cited by 185

Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene.

Keane, M. M., Rivero-Lezcano, O. M., Mitchell, J. A., Robbins, K. C., & Lipkowitz, S. (1995) · PubMed · Cited by 182

Cellular Inhibitors of Apoptosis Proteins cIAP1 and cIAP2 Are Required for Efficient Caspase-1 Activation by the Inflammasome

Labbè, K., McIntire, C. R., Doiron, K., LeBlanc, P. M., & Saleh, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.10.016 · Cited by 180

NF-κB Is Essential for Induction of CYLD, the Negative Regulator of NF-κB

Jono, H., Lim, J. H., Chen, L. F., Xu, H., Trompouki, E., Pan, Z. K., Mosialos, G., & Li, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406638200 · Cited by 180

A spontaneous mutation characterized by chronic proliferative dermatitis in C57BL mice.

HogenEsch, H., Gijbels, M. J., Offerman, E. H., van der Hooft, J. J. J., van Bekkum, D. W., & ZURCHER, C. (1993) · PubMed Central · Cited by 176

K33-Linked Polyubiquitination of T Cell Receptor-ζ Regulates Proteolysis-Independent T Cell Signaling

Huang, H., Jeon, M., Liao, L., Yang, C., Elly, C., Yates, J. R., & Liu, Y. (2010) · Immunity · doi:10.1016/j.immuni.2010.07.002 · Cited by 174

Structure of the A20 OTU domain and mechanistic insights into deubiquitination

Komander, D., & Barford, D. (2007) · Biochemical Journal · doi:10.1042/bj20071399 · Cited by 173

The Peripheral Deletion of Autoreactive CD8+ T Cells Induced by Cross-presentation of Self-antigens Involves Signaling through CD95 (Fas, Apo-1)

Kurts, C., Heath, W. R., Kosaka, H., Miller, J. F. A. P., & Carbone, F. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.2.415 · Cited by 170

Linear ubiquitination: a newly discovered regulator of cell signalling

Rieser, E., Cordier, S. M., & Walczak, H. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.11.007 · Cited by 166

dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8

Estornes, Y., Toscano, F., Virard, F., Jacquemin, G., Pierrot, A., Vanbervliet, B., Bonnin, M., Lalaoui, N., Mercier‐Gouy, P., Pachéco, Y., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.22 · Cited by 164

Inflammatory cardiac valvulitis in TAX1BP1‐deficient mice through selective NF‐κB activation

Iha, H., Péloponèse, J., Verstrepen, L., Zapart, G., Ikeda, F., Smith, C. D., Starost, M. F., Yedavalli, V. R. K., Heyninck, K., Đikić, I., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.5 · Cited by 156

Localization of the APECED protein in distinct nuclear structures

Björses, P. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.2.259 · Cited by 156

Disease‐causing mutations in the XIAP BIR2 domain impair NOD2‐dependent immune signalling

Damgaard, R. B., Fiil, B. K., Speckmann, C., Yabal, M., Stadt, U. Z., Bekker‐Jensen, S., Jost, P. J., Ehl, S. R., Mailand, N., & Gyrd‐Hansen, M. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201303090 · Cited by 152

The E3 Ubiquitin Ligase GRAIL Regulates T Cell Tolerance and Regulatory T Cell Function by Mediating T Cell Receptor-CD3 Degradation

Nurieva, R., Zheng, S., Jin, W., Chung, Y., Zhang, Y., Martínez, G., Reynolds, J. M., Wang, S.-L., Lin, X., Sun, S., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.05.002 · Cited by 150

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription

Colleran, A., Collins, P. E., O’Carroll, C., Ahmed, A., Mao, X., McManus, B., Kiely, P. A., Burstein, E., & Carmody, R. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208446110 · Cited by 150

An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains

Licchesi, J. D. F., Mieszczanek, J., Mevissen, T. E. T., Rutherford, T. J., Akutsu, M., Virdee, S., Oualid, F. E., Chin, J. W., Ovaa, H., Bienz, M., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2169 · Cited by 148

Degradation of Bcl10 Induced by T-Cell Activation Negatively Regulates NF-κB Signaling

Scharschmidt, E., Wegener, E., Heissmeyer, V., Rao, A., & Krappmann, D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.3860-3873.2004 · Cited by 145

AIRE Functions As an E3 Ubiquitin Ligase

Uchida, D., Hatakeyama, S., Matsushima, A., Han, H., Ishido, S., Hotta, H., Kudoh, J., Shimizu, N., Doucas, V., Nakayama, K. I., et al. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20031291 · Cited by 145

Aire and T cell Development

Anderson, M. S., & Su, M. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.11.007 · Cited by 141

Ubiquitin-Specific Protease 25 Regulates TLR4-Dependent Innate Immune Responses Through Deubiquitination of the Adaptor Protein TRAF3

Zhong, B., Liu, X., Wang, X., Liu, X., Li, H., Darnay, B. G., Lin, X., Sun, S., & Dong, C. (2013) · Science Signaling · doi:10.1126/scisignal.2003708 · Cited by 141

Efficient Internalization of MHC I Requires Lysine‐11 and Lysine‐63 Mixed Linkage Polyubiquitin Chains

Boname, J. M., Thomas, M., Stagg, H. R., Xu, P., Peng, J., & Lehner, P. J. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.01011.x · Cited by 136

Virus-triggered Ubiquitination of TRAF3/6 by cIAP1/2 Is Essential for Induction of Interferon-β (IFN-β) and Cellular Antiviral Response

Mao, A., Li, S., Zhong, B., Li, Y., Yan, J., Li, Q., Teng, C., & Shu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071043 · Cited by 134

Defective immune responses in mice lacking LUBAC‐mediated linear ubiquitination in B cells

Sasaki, Y., Sano, S., Nakahara, M., Murata, S., Kometani, K., Aiba, Y., Sakamoto, S., Watanabe, Y., Tanaka, K., Kurosaki, T., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.184 · Cited by 133

Regulation of IκB Kinase-related Kinases and Antiviral Responses by Tumor Suppressor CYLD

Zhang, M., Wu, X., Lee, A. J., Jin, W., Chang, M., Wright, A., Imaizumi, T., & Sun, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801451200 · Cited by 131

Molecular control of the NEMO family of ubiquitin-binding proteins

Clark, K., Nanda, S. K., & Cohen, P. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3644 · Cited by 123

Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs

Silke, J., & Brink, R. A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.114 · Cited by 121

Linear Ubiquitination of NEMO Negatively Regulates the Interferon Antiviral Response through Disruption of the MAVS-TRAF3 Complex

Belgnaoui, S. M., Paz, S., Samuel, S., Goulet, M.-L., Sun, Q., Kikkert, M., Iwaï, K., Đikić, I., Hiscott, J. B., & Lin, R. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.06.009 · Cited by 119

Targeting pattern recognition receptors in cancer immunotherapy

Goutagny, N., Estornes, Y., Hasan, U. A., Lebecque, S., & Caux, C. (2012) · Targeted Oncology · doi:10.1007/s11523-012-0213-1 · Cited by 113

Following Ariadne's thread: a new perspective on RBR ubiquitin ligases

Wenzel, D. M., & Klevit, R. E. (2012) · BMC Biology · doi:10.1186/1741-7007-10-24 · Cited by 106

BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs

Mathew, R. S., Seiler, M. P., Scanlon, S. T., Mao, A., Constantinides, M. G., Bertozzi-Villa, C., Singer, J. D., & Bendelac, A. S. (2012) · Nature · doi:10.1038/nature11548 · Cited by 105

Emerging Role of Ubiquitination in Antiviral RIG-I Signaling

Maelfait, J., & Beyaert, R. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05012-11 · Cited by 105

XIAP Regulates Cytosol-Specific Innate Immunity to Listeria Infection

Bauler, L. D., Duckett, C. S., & O’Riordan, M. X. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000142 · Cited by 98

NMR Structure of the First PHD Finger of Autoimmune Regulator Protein (AIRE1)

Bottomley, M. J., Stier, G., Pennacchini, D., Legube, G., Simon, B., Akhtar, A., Sattler, M., & Musco, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413959200 · Cited by 98

The Gene Related to Anergy in Lymphocytes, an E3 Ubiquitin Ligase, Is Necessary for Anergy Induction in CD4 T Cells

Seroogy, C. M., Soares, L. R. B., Ranheim, E. A., Su, L., Holness, C. L. L., Bloom, D. D., & Fathman, C. G. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.1.79 · Cited by 96

Signature biomarkers in Crohn's disease: toward a molecular classification

Arsenescu, R. I., Bruno, M., Rogier, E. W., Stefka, A. T., McMahan, A., Wright, T. B., Nasser, M. S., de Villiers, W. J. S., & Kaetzel, C. S. (2008) · Mucosal Immunology · doi:10.1038/mi.2008.32 · Cited by 78

Development, organization and function of the thymic medulla in normal, immunodeficient or autoimmune mice

Naquet, P., Naspetti, M., & Boyd, R. L. (1999) · Seminars in Immunology · doi:10.1006/smim.1998.0149 · Cited by 78

Immunosuppression induced by immature dendritic cells is mediated by TGF‐β/IL‐10 double‐positive CD4+ regulatory T cells

Cools, N., Tendeloo, V. F. V., Smits, E., Lenjou, M., Nijs, G., Bockstaele, D. R. V., Berneman, Z. N., & Ponsaerts, P. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00084.x · Cited by 77

Toll-like receptor 3 agonist complexed with cationic liposome augments vaccine-elicited antitumor immunity by enhancing TLR3–IRF3 signaling and type I interferons in dendritic cells

Wang, C., Zhuang, Y., Zhang, Y., Luo, Z., Gao, N., Li, P., Pan, H., Cai, L., & Ma, Y. (2012) · Vaccine · doi:10.1016/j.vaccine.2012.05.027 · Cited by 73

The Single Subunit Transmembrane E3 Ligase Gene Related to Anergy in Lymphocytes (GRAIL) Captures and Then Ubiquitinates Transmembrane Proteins across the Cell Membrane

Lineberry, N. B., Su, L., Soares, L. R. B., & Fathman, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805092200 · Cited by 73

To fight or die — inhibitor of apoptosis proteins at the crossroad of innate immunity and death

Lopez, J. S., & Meier, P. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.08.025 · Cited by 71

The role of E3 ligases in autoimmunity and the regulation of autoreactive T cells

Lin, A. E., & Mak, T. W. (2007) · Current Opinion in Immunology · doi:10.1016/j.coi.2007.10.002 · Cited by 69

GRAIL Is Up-regulated in CD4+ CD25+ T Regulatory Cells and Is Sufficient for Conversion of T Cells to a Regulatory Phenotype

MacKenzie, D. A., Schartner, J. M., Lin, J. T., Timmel, A., Jennens-Clough, M. L., Fathman, C. G., & Seroogy, C. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m604192200 · Cited by 68

Contribution of Lysine 11-linked Ubiquitination to MIR2-mediated Major Histocompatibility Complex Class I Internalization

Gotō, E., Yamanaka, Y., Ishikawa, A., Aoki-Kawasumi, M., Mito-Yoshida, M., Ohmura‐Hoshino, M., Matsuki, Y., Kajikawa, M., Hirano, H., & Ishido, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.112763 · Cited by 66

Absence of Peyer’s Patches and Abnormal Lymphoid Architecture in Chronic Proliferative Dermatitis ( cpdm/cpdm ) Mice

HogenEsch, H., Janke, S., Boggess, D., & Sundberg, J. P. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.7.3890 · Cited by 64

The E3 ubiquitin ligase Itch in T cell activation, differentiation, and tolerance

Liu, Y. (2007) · Seminars in Immunology · doi:10.1016/j.smim.2007.02.003 · Cited by 60

Cutting Edge: The Transmembrane E3 Ligase GRAIL Ubiquitinates the Costimulatory Molecule CD40 Ligand during the Induction of T Cell Anergy

Lineberry, N. B., Su, L., Lin, J. T., Coffey, G., Seroogy, C. M., & Fathman, C. G. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.3.1622 · Cited by 56

Solution Structure of N-TRADD and Characterization of the Interaction of N-TRADD and C-TRAF2, a Key Step in the TNFR1 Signaling Pathway

Tsao, D. H. H., McDonagh, T., Telliez, J., Hsu, S., Malakian, K., Xu, G.-Y., & Lin, L.-L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80270-1 · Cited by 55

Induction of hyporesponsiveness to intact foreign protein via retroviral-mediated gene expression: The IgG scaffold is important for induction and maintenance of immune hyporesponsiveness

Kang, Y., Melo, M. E. F., Deng, E., Tisch, R., El-Amine, M., & Scott, D. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8609 · Cited by 55

NEMO oligomerization and its ubiquitin-binding properties

Ivins, F. J., Montgomery, M., Smith, S. J., Morris-Davies, A. C., Taylor, I. A., & Rittinger, K. (2009) · Biochemical Journal · doi:10.1042/bj20090427 · Cited by 52

TNF and ROS crosstalk in inflammation

Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008

Reactive Oxygen Species: Drivers of Physiological and Pathological Processes

Checa, J., & Aran, J. M. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s275595 · Cited by 1,068

E3 ubiquitin ligases: styles, structures and functions

Yang, Q., Zhao, J., Chen, D., & Wang, Y. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00043-2 · Cited by 435

Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

Qiu, J., Sheedlo, M. J., Yu, K., Tan, Y., Nakayasu, E. S., Das, C., Liu, X., & Luo, Z. (2016) · Nature · doi:10.1038/nature17657 · Cited by 359

The K48-K63 Branched Ubiquitin Chain Regulates NF-κB Signaling

Ohtake, F., Saeki, Y., Ishido, S., Kanno, J., & Tanaka, K. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.014 · Cited by 350

Review “Ubiquitylation: mechanism and functions ” Review series Ubiquitin in the immune system

Zinngrebe, J., Montinaro, A., Peltzer, N., & Walczak, H. (2013)

Ubiquitin signaling in immune responses

Hu, H., & Sun, S. (2016) · Cell Research · doi:10.1038/cr.2016.40 · Cited by 492

The role of ubiquitylation in immune defence and pathogen evasion

Jiang, X., & Chen, Z. J. (2011) · Nature reviews. Immunology · doi:10.1038/nri3111 · Cited by 352

Ubiquitylation in innate and adaptive immunity

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

The Ubiquitin System in Immune Regulation

Park, Y., Jin, H., Aki, D., Lee, J., & Liu, Y. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800147-9.00002-9 · Cited by 71