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 14,244 · see citing works

Pathogen Recognition and Innate Immunity

Akira, S., Uematsu, S., & Takeuchi, O. (2006) · Cell · doi:10.1016/j.cell.2006.02.015 · Cited by 11,974 · see citing works

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 · see citing works

Pattern Recognition Receptors and Inflammation

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

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 · see citing works

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 · see citing works

The Danger Model: A Renewed Sense of Self

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

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 · see citing works

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 · see citing works

Recognition of microorganisms and activation of the immune response

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 2,486 · see citing works

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

Anderson, M. S., Venanzi, E. S., Klein, L., Chen, Z., Berzins, S. P., Turley, S. J., von Boehmer, H., Bronson, R. T., Dierich, A., Benoist, C. O., et al. (2002) · Science · doi:10.1126/science.1075958 · Cited by 2,474 · see citing works

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 · see citing works

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 2,369 · see citing works

Proteomic analysis of post-translational modifications

Mann, M., & Jensen, O. N. (2003) · Nature Biotechnology · doi:10.1038/nbt0303-255 · Cited by 2,136 · see citing works

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 2,106 · see citing works

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 · see citing works

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 · 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

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 1,776 · see citing works

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 · see citing works

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 · see citing works

T cell anergy

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

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 · see citing works

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 · see citing works

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 1,352 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,091 · see citing works

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 1,063 · see citing works

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 1,030 · 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

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 998 · see citing works

Building ubiquitin chains: E2 enzymes at work

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

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 · see citing works

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 · 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

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 943 · see citing works

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 · see citing works

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 921 · see citing works

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 890 · see citing works

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 · see citing works

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 859 · see citing works

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 855 · see citing works

Ubiquitin-binding domains

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

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 772 · 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

Control of B-cell responses by Toll-like receptors

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

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 745 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 642 · see citing works

Ubiquitylation in innate and adaptive immunity

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

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 · see citing works

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 · see citing works

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 615 · see citing works

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 · see citing works

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 607 · see citing works

Ubiquitin-binding domains

Hurley, J. H., Lee, S., & Prag, G. (2006) · Biochemical Journal · doi:10.1042/bj20061138 · Cited by 601 · see citing works

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 595 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 550 · see citing works

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 550 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 489 · see citing works

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 482 · see citing works

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 472 · see citing works

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 · see citing works

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

Boisson, B., Laplantine, E., Prando, C., Giliani, S. C., 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 470 · see citing works

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 467 · see citing works

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 · see citing works

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 · see citing works

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 433 · see citing works

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 · see citing works

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 · see citing works

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 394 · see citing works

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 · see citing works

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 388 · see citing works

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 · see citing works

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 379 · see citing works

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 · see citing works

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 · see citing works

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 350 · see citing works

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 350 · see citing works

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 349 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 338 · see citing works

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 · see citing works

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 · see citing works

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 324 · see citing works

"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 · see citing works

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 310 · see citing works

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 · see citing works

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 302 · see citing works

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 · see citing works

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 · see citing works

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 288 · see citing works

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 · see citing works

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 · see citing works

Untitled work

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

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 280 · see citing works

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 280 · see citing works

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 · see citing works

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 · see citing works

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 267 · see citing works

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 · see citing works

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 265 · see citing works

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 260 · see citing works

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 · see citing works

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 256 · see citing works

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 · see citing works

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 253 · see citing works

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 252 · see citing works

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 246 · see citing works

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 · see citing works

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 · see citing works

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

Nishikawa, H., Ooka, S., Sato, K., Arima, Κ., Okamoto, J., Klevit, R. E., Fukuda, M., & Ohta, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308540200 · Cited by 238 · see citing works

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 · see citing works

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 · see citing works

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 220 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 210 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 196 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 184 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Structure of the A20 OTU domain and mechanistic insights into deubiquitination

Komander, D., & Barford, D. (2007) · Biochemical Journal · doi:10.1042/bj20071399 · Cited by 170 · see citing works

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 · see citing works

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 169 · see citing works

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 · see citing works

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 159 · see citing works

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 · see citing works

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 153 · see citing works

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 · see citing works

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 148 · see citing works

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 · see citing works

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 147 · see citing works

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 · see citing works

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 · see citing works

Aire and T cell development

Anderson, M. S., & Su, M. A. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.11.007 · Cited by 143 · see citing works

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 · see citing works

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 · see citing works

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

Zhong, B., Liu, X.-K., Wang, X., Liu, X.-D., Li, H., Darnay, B., Lin, X., Sun, S.-C., & Dong, C. (2013) · Science Signaling · doi:10.1126/scisignal.2003708 · Cited by 129 · see citing works

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 128 · see citing works

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 126 · see citing works

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 · see citing works

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 119 · see citing works

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 117 · see citing works

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 109 · see citing works

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 · see citing works

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 102 · see citing works

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 · see citing works

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 98 · see citing works

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 97 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 72 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 50 · see citing works

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 · see citing works

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 1,022 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

New insights into the evasion of host innate immunity by Mycobacterium tuberculosis

Chai, Q., Wang, L., Liu, C. H., & Ge, B. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0502-z · Cited by 336 · see citing works

LUBAC-Recruited CYLD and A20 Regulate Gene Activation and Cell Death by Exerting Opposing Effects on Linear Ubiquitin in Signaling Complexes

Dráber, P., Kupka, S., Reichert, M., Draberova, H., Lafont, É., de Miguel, D., Spilgies, L. M., Šurinová, S., Taraborrelli, L., Hartwig, T., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.009 · Cited by 288 · see citing works

HOIP Deficiency Causes Embryonic Lethality by Aberrant TNFR1-Mediated Endothelial Cell Death

Peltzer, N., Rieser, E., Taraborrelli, L., Draber, P., Darding, M., Pernaute, B., Shimizu, Y., Sarr, A., Draberova, H., Montinaro, A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.066 · Cited by 257 · see citing works

Post-translational regulation of inflammasomes

Yang, J., Liu, Z., & Xiao, T. S. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.29 · Cited by 201 · see citing works

Dynamic control of type I IFN signalling by an integrated network of negative regulators

Porritt, R. A., & Hertzog, P. J. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.02.002 · Cited by 198 · see citing works

Structure-guided development of a potent and selective non-covalent active-site inhibitor of USP7.

Lamberto, I., Liu, X., Seo, H.-S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.003 · Cited by 192 · see citing works

Holding RIPK1 on the Ubiquitin Leash in TNFR1 Signaling

Peltzer, N., Darding, M., & Walczak, H. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.01.006 · Cited by 184 · see citing works

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 · see citing works

USP19 modulates autophagy and antiviral immune responses by deubiquitinating Beclin‐1

Jin, S., Tian, S., Chen, Y., Zhang, C., Xie, W., Xia, X., Cui, J., & Wang, R. (2016) · The EMBO Journal · doi:10.15252/embj.201593596 · Cited by 174 · see citing works

The PB1 protein of influenza A virus inhibits the innate immune response by targeting MAVS for NBR1-mediated selective autophagic degradation

Zeng, Y., Xu, S., Wei, Y., Zhang, X., Wang, Q., Jia, Y., Wang, W., Han, L., Chen, Z., Wang, Z., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009300 · Cited by 151 · see citing works

Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis

Nakazawa, S., Oikawa, D., Ishii, R., Ayaki, T., Takahashi, H., Takeda, H., Ishitani, R., Kamei, K., Takeyoshi, I., Kawakami, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms12547 · Cited by 151 · see citing works

TRIM25 in the Regulation of the Antiviral Innate Immunity

Martin‐Vicente, M., Medrano, L. M., Resino, S., García‐Sastre, A., & Martínez, I. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01187 · Cited by 148 · see citing works

RBR E3‐ligases at work

Smit, J. J., & Sixma, T. K. (2014) · EMBO Reports · doi:10.1002/embr.201338166 · Cited by 146 · see citing works

Ubiquitin-Mediated Regulation of RIPK1 Kinase Activity Independent of IKK and MK2

Annibaldi, A., John, S. W., Berghe, T. V., Swatek, K. N., Ruan, J., Liccardi, G., Bianchi, K., Elliott, P. R., Choi, S. M., Coillie, S. V., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.027 · Cited by 145 · see citing works

Linear ubiquitination in immunity

Shimizu, Y., Taraborrelli, L., & Walczak, H. (2015) · Immunological Reviews · doi:10.1111/imr.12309 · Cited by 135 · see citing works

SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes

Kupka, S., De Miguel, D., Draber, P., Martino, L., Surinova, S., Rittinger, K., & Walczak, H. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.086 · Cited by 135 · see citing works

ARIH2 Ubiquitinates NLRP3 and Negatively Regulates NLRP3 Inflammasome Activation in Macrophages

Kawashima, A., Karasawa, T., Tago, K., Kimura, H. J., Kamata, R., Usui‐Kawanishi, F., Watanabe, S., Ohta, S., Funakoshi‐Tago, M., Yanagisawa, K., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700184 · Cited by 140 · see citing works

Ubiquitin enzymes in the regulation of immune responses

Ebner, P., Versteeg, G. A., & Ikeda, F. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1325829 · Cited by 139 · see citing works

K63 ubiquitination in immune signaling

Madiraju, C., Novack, J. P., Reed, J. C., & Matsuzawa, S. (2022) · Trends in Immunology · doi:10.1016/j.it.2021.12.005 · Cited by 136 · see citing works

PRR-signaling pathways: Learning from microbial tactics

Sellge, G., & Kufer, T. A. (2015) · Seminars in Immunology · doi:10.1016/j.smim.2015.03.009 · Cited by 129 · see citing works

Diverse ubiquitin linkages regulate RIP kinases-mediated inflammatory and cell death signaling

Witt, A., & Vucic, D. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.33 · Cited by 126 · see citing works

The ubiquitin hybrid gene UBA52 regulates ubiquitination of ribosome and sustains embryonic development

Kobayashi, M., Oshima, S., Maeyashiki, C., Nibe, Y., Otsubo, K., Matsuzawa, Y., Nemoto, Y., Nagaishi, T., Okamoto, R., Tsuchiya, K., et al. (2016) · Scientific Reports · doi:10.1038/srep36780 · Cited by 123 · see citing works

The ubiquitin system: a critical regulator of innate immunity and pathogen–host interactions

Li, J., Chai, Q., & Liu, C. H. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.40 · Cited by 115 · see citing works

Roles of linear ubiquitinylation, a crucial regulator of NF ‐κB and cell death, in the immune system

Sasaki, K., & Iwaï, K. (2015) · Immunological Reviews · doi:10.1111/imr.12308 · Cited by 110 · see citing works

The many substrates and functions of NEDD4-1

Huang, X., Chen, J., Cao, W., Yang, L., Chen, Q., He, J., Yi, Q., Huang, H., Zhang, E., & Cai, Z. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2142-8 · Cited by 114 · see citing works

Protein Turnover in Aging and Longevity

Basisty, N., Meyer, J. G., & Schilling, B. (2018) · PROTEOMICS · doi:10.1002/pmic.201700108 · Cited by 112 · see citing works

Regulation of C-Type Lectin Receptor-Mediated Antifungal Immunity

Tang, J., Lin, G., Langdon, W. Y., Tao, L., & Zhang, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00123 · Cited by 109 · see citing works

USP18 negatively regulates NF-κB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms

Yang, Z., Xian, H., Hu, J., Tian, S., Qin, Y., Wang, R., & Cui, J. (2015) · Scientific Reports · doi:10.1038/srep12738 · Cited by 108 · see citing works

The HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC

Fuseya, Y., Fujita, H., Kim, M., Ohtake, F., Nishide, A., Sasaki, K., Saeki, Y., Tanaka, K., Takahashi, R., & Iwaï, K. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0517-9 · Cited by 84 · see citing works

Atypical ubiquitin E3 ligase complex Skp1-Pam-Fbxo45 controls the core epithelial-to-mesenchymal transition-inducing transcription factors

Xu, M., Zhu, C., Zhao, X., Chen, C., Zhang, H., Yuan, H., Deng, R., Dou, J., Wang, Y., Huang, J. J., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2825 · Cited by 87 · see citing works

An E1–E2 fusion protein primes antiviral immune signalling in bacteria

Ledvina, H. E., Ye, Q., Gu, Y., Sullivan, A. E., Quan, Y., Lau, R. K., Zhou, H., Corbett, K. D., & Whiteley, A. T. (2023) · Nature · doi:10.1038/s41586-022-05647-4 · Cited by 83 · see citing works

RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation

Yang, B., Liu, Y., Cui, Y., Song, D., Zhang, G., Ma, S., Liu, Y., Chen, M., Chen, F., Wang, H., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008387 · Cited by 78 · see citing works

LRRC25 Functions as an Inhibitor of NF-κB Signaling Pathway by Promoting p65/RelA for Autophagic Degradation

Feng, Y., Duan, T., Du, Y., Jin, S., Wang, M., Cui, J., & Wang, R. (2017) · Scientific Reports · doi:10.1038/s41598-017-12573-3 · Cited by 77 · see citing works

Structure and Function of Viral Deubiquitinating Enzymes

Bailey-Elkin, B. A., Knaap, R. C. M., Kikkert, M., & Mark, B. L. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.06.010 · Cited by 77 · see citing works

Glycogen synthase kinase 3β ubiquitination by TRAF6 regulates TLR3-mediated pro-inflammatory cytokine production

Ko, R., Park, J. H., Ha, H., Choi, Y., & Lee, S. Y. (2015) · Nature Communications · doi:10.1038/ncomms7765 · Cited by 75 · see citing works

Innate and Adaptive Immune Responses in Chronic HCV Infection

Dustin, L. B. (2015) · Current Drug Targets · doi:10.2174/1389450116666150825110532 · Cited by 72 · see citing works

Opsonic Phagocytosis in Chronic Obstructive Pulmonary Disease Is Enhanced by Nrf2 Agonists

Bewley, M. A., Budd, R. C., Ryan, E. M., Cole, J., Collini, P., Marshall, J. L., Kolsum, U., Beech, G., Emes, R. D., Tcherniaeva, I., et al. (2018) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201705-0903oc · Cited by 72 · see citing works

The function and regulation of OTU deubiquitinases

Du, J., Fu, L., Sui, Y., & Zhang, L. (2019) · Frontiers of Medicine · doi:10.1007/s11684-019-0734-4 · Cited by 72 · see citing works

Ubiquitination of NLRP3 by gp78/Insig-1 restrains NLRP3 inflammasome activation

Xu, T., Yu, W., Fang, H., Wang, Z., Chi, Z.-X., Guo, X.-C., Jiang, D., Zhang, K., Chen, S., Li, M.-B., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00947-8 · Cited by 68 · see citing works

Dietary Methionine Improves the European Seabass (Dicentrarchus labrax) Immune Status, Inflammatory Response, and Disease Resistance

Machado, M., Azeredo, R., Fontinha, F., Fernández-Boo, S., Conceição, L. E. C., Dias, J. P., & Costas, B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02672 · Cited by 70 · see citing works

Ubiquitin‐dependent regulation of Foxp3 and Treg function

Barbi, J. J., Pardoll, D. M., & Pan, F. (2015) · Immunological Reviews · doi:10.1111/imr.12312 · Cited by 68 · see citing works

Acetylation, Phosphorylation, Ubiquitination (Oh My!): Following Post-Translational Modifications on the Ubiquitin Road

Lacoursiere, R. E., Hadi, D., & Shaw, G. S. (2022) · Biomolecules · doi:10.3390/biom12030467 · Cited by 70 · see citing works

Lys29-linkage of ASK1 by Skp1−Cullin 1−Fbxo21 ubiquitin ligase complex is required for antiviral innate response

Zhou, Y., Chen, T., Li, X., Yang, M., Tang, S., Zhu, X., Gu, Y. H., Su, X., Meng, X., Li, W., et al. (2016) · eLife · doi:10.7554/elife.14087 · Cited by 67 · see citing works

Molecular glue-mediated targeted protein degradation: A novel strategy in small-molecule drug development

Tan, X., Huang, Z., Pei, H., Jia, Z., & Zheng, J. (2024) · iScience · doi:10.1016/j.isci.2024.110712 · Cited by 66 · see citing works

Emerging drug development technologies targeting ubiquitination for cancer therapeutics

Veggiani, G., Gerpe, M. C. R., Sidhu, S. S., & Zhang, W. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.03.003 · Cited by 64 · see citing works

NEDD4 lactylation promotes APAP induced liver injury through Caspase11 dependent non-canonical pyroptosis

Li, Q., Zhang, F., Wang, H., Tong, Y., Fu, Y., Wu, K., Li, J., Wang, C., Wang, Z., Jia, Y., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.91284 · Cited by 66 · see citing works

HECTD3 mediates TRAF3 polyubiquitination and type I interferon induction during bacterial infection

Li, F., Li, Y., Liang, H., Xu, T., Kong, Y., Huang, M., Xiao, J., Chen, X., Xia, H., Wu, Y., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120406 · Cited by 64 · see citing works

Interplay between Inflammation and Stemness in Cancer Cells: The Role of Toll-Like Receptor Signaling

Yeh, D.-W., Huang, L.-R., Chen, Y.-W., Huang, C.-Y. F., & Chuang, T.-H. (2016) · Journal of Immunological Research · doi:10.1155/2016/4368101 · Cited by 58 · see citing works

The Molecular Links between Cell Death and Inflammasome

Lee, K. H., & Kang, T. (2019) · Cells · doi:10.3390/cells8091057 · Cited by 62 · see citing works

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

Liu, Z., Gong, Z., Jiang, W.-X., Yang, J., Zhu, W.-K., Guo, D.-C., Zhang, W.-P., Liu, M.-L., & Tang, C. (2015) · eLife · doi:10.7554/elife.05767 · Cited by 60 · see citing works

Ubiquitin in inflammation: the right linkage makes all the difference

Corn, J. E., & Vucic, D. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2808 · Cited by 60 · see citing works

The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1

Middleton, A. J., Budhidarmo, R., Das, A., Zhu, J., Foglizzo, M., Mace, P. D., & Day, C. L. (2017) · Nature Communications · doi:10.1038/s41467-017-01665-3 · Cited by 59 · see citing works

Epigenetic Regulation of Neuroinflammation in Alzheimer’s Disease

Ma, Y., Wang, W., Liu, S., Qiao, X., Xing, Y., Zhou, Q., & Zhang, Z. (2023) · Cells · doi:10.3390/cells13010079 · Cited by 57 · see citing works

A quantitative genome-wide RNAi screen in C. elegans for antifungal innate immunity genes

Zugasti, O., Thakur, N., Belougne, J., Squiban, B., Kurz, C. L., Soulé, J., Omi, S., Tichit, L., Pujol, N., & Ewbank, J. J. (2016) · BMC Biology · doi:10.1186/s12915-016-0256-3 · Cited by 56 · see citing works

Death Receptors and Their Ligands in Inflammatory Disease and CancerPreprint

Annibaldi, A., & Walczak, H. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036384 · Cited by 59 · see citing works

Ubiquitin Ligases in Cancer Immunotherapy – Balancing Antitumor and Autoimmunity

Fujita, Y., Tinoco, R., Li, Y., Senft, D., & Ronai, Z. A. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.02.002 · Cited by 53 · see citing works

Essential role of HCMV deubiquitinase in promoting oncogenesis by targeting anti-viral innate immune signaling pathways

Kumari, P., Saha, I., Narayanan, A., Narayanan, S., Takaoka, A., Kumar, N. S., Tailor, P. B., & Kumar, H. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.461 · Cited by 53 · see citing works

The deubiquitinating enzyme UCHL1 negatively regulates the immunosuppressive capacity and survival of multipotent mesenchymal stromal cells

Gu, Y., Ding, X., Huang, J., Xue, M., Zhang, J., Wang, Q., Yu, H., Wang, Y., Zhao, F., Wang, H., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0532-y · Cited by 53 · see citing works

The Ubiquitination System within Bacterial Host–Pathogen Interactions

Vozandychova, V., Stojková, P., Hercík, K., Řehulka, P., & Stulík, J. (2021) · Microorganisms · doi:10.3390/microorganisms9030638 · Cited by 52 · see citing works

Downregulation of COMMD1 by miR-205 promotes a positive feedback loop for amplifying inflammatory- and stemness-associated properties of cancer cells

Yeh, D.-W., Chen, Y.-S., Lai, C.-Y., Liu, Y.-L., Lu, C.-H., Lo, J., Chen, L., Hsu, L.-C., Luo, Y., Xiang, R., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.147 · Cited by 52 · see citing works

Immune control and failure in HCV infection—tipping the balance

Dustin, L. B., Cashman, S. B., & Laidlaw, S. M. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.4ri0214-126r · Cited by 51 · see citing works

USP1-regulated reciprocal differentiation of Th17 cells and Treg cells by deubiquitinating and stabilizing TAZ

Zhu, X., Wang, P., Zhan, X., Zhang, Y., Sheng, J., He, S., Chen, Y., Nie, D., You, X., Mai, H., et al. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00969-9 · Cited by 49 · see citing works

Post-Translational Modifications of RelB NF-κB Subunit and Associated Functions

Baud, V., & Collares, D. (2016) · Cells · doi:10.3390/cells5020022 · Cited by 49 · see citing works

Ubiquitin carboxyl-terminal hydrolase-L5 promotes TGFβ-1 signaling by de-ubiquitinating and stabilizing Smad2/Smad3 in pulmonary fibrosis

Ling, N., Jacko, A. M., Tan, J., Wang, D., Zhao, J., Kass, D. J., Ma, H., & Zhao, Y. (2016) · Scientific Reports · doi:10.1038/srep33116 · Cited by 48 · see citing works

The emerging roles of non-canonical ubiquitination in proteostasis and beyond

Akizuki, Y., Kaypee, S., Ohtake, F., & Ikeda, F. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311171 · Cited by 45 · see citing works

HOIL1 Is Essential for the Induction of Type I and III Interferons by MDA5 and Regulates Persistent Murine Norovirus Infection

MacDuff, D. A., Baldridge, M. T., Qaqish, A., Nice, T. J., Darbandi, A. D., Hartley, V. L., Peterson, S. T., Miner, J. J., Iwaï, K., & Virgin, H. W. (2018) · Journal of Virology · doi:10.1128/jvi.01368-18 · Cited by 43 · see citing works

E3 ubiquitin ligase Nedd4 is a key negative regulator for non-canonical inflammasome activation

Liu, Q., Zhang, S., Sun, Z., Guo, X. P., & Zhou, H. M. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0308-7 · Cited by 45 · see citing works

Degradation of CCNB1 mediated by APC11 through UBA52 ubiquitination promotes cell cycle progression and proliferation of non-small cell lung cancer cells.

Wang, F., Chen, X., Yu, X., & Lin, Q. (2019) · PubMed Central · Cited by 43 · see citing works

Ubiquitinated AIF is a major mediator of hypoxia-induced mitochondrial dysfunction and pulmonary artery smooth muscle cell proliferation

Ma, C., Wang, X., He, S., Zhang, L., Bai, J., Qu, L., Qi, J., Zheng, X., Zhu, X., Mei, J., et al. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00744-3 · Cited by 42 · see citing works

Molecular mechanism and cellular function of MHCII ubiquitination

Oh, J., & Shin, J. (2015) · Immunological Reviews · doi:10.1111/imr.12303 · Cited by 41 · see citing works

K27-linked noncanonic ubiquitination in immune regulation

Zhou, Q., & Zhang, J. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.4ru0620-397rr · Cited by 44 · see citing works

Zebrafish F-box Protein fbxo3 Negatively Regulates Antiviral Response through Promoting K27-Linked Polyubiquitination of the Transcription Factors irf3 and irf7

Li, Z., Fan, S., Wang, J., Chen, X., Liao, Q., Liu, X., Ouyang, G., Cao, H., & Xiao, W. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000305 · Cited by 41 · see citing works

Modulating the Ubiquitin–Proteasome System: A Therapeutic Strategy for Autoimmune Diseases

Yadav, D., Lee, J. Y., Puranik, N., Chauhan, P., Chavda, V. K., Jin, J., & Lee, P. C.-W. (2022) · Cells · doi:10.3390/cells11071093 · Cited by 41 · see citing works

The NEDD4‐1 E3 ubiquitin ligase: A potential molecular target for bortezomib sensitivity in multiple myeloma

Huang, X., Gu, H., Zhang, E., Chen, Q., Cao, W., Yan, H., Chen, J., Yang, L., Lv, N., He, J., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32615 · Cited by 38 · see citing works

Identification and validation of selective deubiquitinase inhibitors

Varca, A. C., Casalena, D. E., Chan, W. C., Hu, B., Magin, R. S., Roberts, R. M., Liu, X., Zhu, H., Seo, H., Dhe‐Paganon, S., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.05.012 · Cited by 37 · see citing works

Identification of Candidate Signature Genes and Key Regulators Associated With Trypanotolerance in the Sheko Breed

Mekonnen, Y. A., Gültas, M., Effa, K., Hanotte, O., & Schmitt, A. O. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01095 · Cited by 37 · see citing works

RNF213 promotes Treg cell differentiation by facilitating K63-linked ubiquitination and nuclear translocation of FOXO1

Yang, X., Zhu, X., Sheng, J., Fu, Y., Nie, D., You, X., Chen, Y., Yang, X., Ling, Q., Zhang, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50392-z · Cited by 39 · see citing works

The E3 ubiquitin ligase MIB2 enhances inflammation by degrading the deubiquitinating enzyme CYLD

Uematsu, A., Kido, K., Takahashi, H., Takahashi, C., Yanagihara, Y., Saeki, N., Yoshida, S. M., Maekawa, M., Honda, M., Kai, T., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010119 · Cited by 38 · see citing works

RNF144A promotes antiviral responses by modulating STING ubiquitination

Yang, B., Pei, J., Chen, L., Wang, Y., Shen, M., Qin, X., Huang, Y., Yang, X., Zhao, X., Ma, S., et al. (2023) · EMBO Reports · doi:10.15252/embr.202357528 · Cited by 35 · see citing works

Systematic analysis of the IL‐17 receptor signalosome reveals a robust regulatory feedback loop

Draberova, H., Janusova, S., Knizkova, D., Šemberová, T., Přibíková, M., Ujevic, A., Harant, K., Knápková, S., Hrdinka, M., Fanfani, V., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104202 · Cited by 34 · see citing works

Zebrafish otud6b Negatively Regulates Antiviral Responses by Suppressing K63-Linked Ubiquitination of irf3 and irf7

Zhou, Z., Cai, X., Zhu, J., Li, Z., Yu, G., Liu, X., Ouyang, G., & Xiao, W. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2000891 · Cited by 36 · see citing works

Compound heterozygous variants in OTULIN are associated with fulminant atypical late‐onset ORAS

Zinngrebe, J., Moepps, B., Monecke, T., Gierschik, P., Schlichtig, F., Barth, T. F. E., Strauß, G., Boldrin, E., Posovszky, C., Schulz, A., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202114901 · Cited by 34 · see citing works

Weighted Gene Co-Expression Network Analysis Based on Stimulation by Lipopolysaccharides and Polyinosinic:polycytidylic Acid Provides a Core Set of Genes for Understanding Hemolymph Immune Response Mechanisms of Amphioctopus fangsiao

Wang, Y., Chen, X., Xu, X., Yang, J., Liu, X., Sun, G., & Li, Z. (2023) · Animals · doi:10.3390/ani14010080 · Cited by 34 · see citing works

UBR5 mediates colorectal cancer chemoresistance by attenuating ferroptosis via Lys 11 ubiquitin-dependent stabilization of Smad3-SLC7A11 signaling

Song, M. L., Huang, S., Wu, X., Zhao, Z., Liu, X., Wu, C., Wang, M., Gao, J., Ke, Z.-F., Ma, X., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103349 · Cited by 33 · see citing works

Ubiquitination regulation of inflammatory responses through NF-κB pathway.

Wu, Y., Kang, J., Zhang, L., Liang, Z., Tang, X., Yan, Y., Qian, H., Zhang, X., Xu, W., & Mao, F. (2018) · PubMed Central · Cited by 33 · see citing works

eIF3k inhibits NF-κB signaling by targeting MyD88 for ATG5-mediated autophagic degradation in teleost fish

Chen, Y., Cao, B., Zheng, W., Sun, Y., & Xu, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101730 · Cited by 33 · see citing works

The NEL Family of Bacterial E3 Ubiquitin Ligases

Bullones-Bolaños, A., Bernal-Bayard, J., & Ramos‐Morales, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147725 · Cited by 33 · see citing works

An IMiD-induced SALL4 degron system for selective degradation of target proteins

Yamanaka, S., Shoya, Y., Matsuoka, S., Nishida-Fukuda, H., Shibata, N., & Sawasaki, T. (2020) · Communications Biology · doi:10.1038/s42003-020-01240-5 · Cited by 29 · see citing works

The molecular dissection of TRIM25’s RNA-binding mechanism provides key insights into its antiviral activity

Álvarez, L., Haubrich, K., Iselin, L., Gillioz, L., Ruscica, V., Lapouge, K., Augsten, S., Huppertz, I., Choudhury, N. R., Simon, B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52918-x · Cited by 32 · see citing works

Ubiquitination as an Efficient Molecular Strategy Employed in Salmonella Infection

Narayanan, L. A., & Edelmann, M. J. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00558 · Cited by 32 · see citing works

Viral deubiquitinases: role in evasion of anti-viral innate immunity

Kumari, P., & Kumar, H. (2017) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2017.1368999 · Cited by 32 · see citing works

Samotolisib Attenuates Acute Liver Injury Through Inhibiting Caspase-11-Mediated Pyroptosis Via Regulating E3 Ubiquitin Ligase Nedd4

Zhao, Y., Wu, D., He, M., Zhang, F., Zhang, T., Liu, T., Li, J., Li, L., & Xu, Y. X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.726198 · Cited by 32 · see citing works

Genomics, Biology, and Human Illness

Oda, H., & Kastner, D. L. (2017) · Rheumatic Disease Clinics of North America · doi:10.1016/j.rdc.2017.04.011 · Cited by 29 · see citing works

Increased A20-E3 ubiquitin ligase interactions in bid-deficient glia attenuate TLR3- and TLR4-induced inflammation

Kinsella, S. M., Fichtner, M. W., Watters, O., König, H., & Prehn, J. H. M. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1143-3 · Cited by 30 · see citing works

Ubiquitinated ligation protein NEDD4L participates in MiR-30a-5p attenuated atherosclerosis by regulating macrophage polarization and lipid metabolism

Song, F., Li, J.-Z., Wu, Y., Wu, W., Wang, Y., & Li, G. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.10.030 · Cited by 30 · see citing works

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 481 · see citing works

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 350 · see citing works

Ubiquitylation in innate and adaptive immunity

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

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 67 · see citing works