Nonproteolytic Functions of Ubiquitin in Cell Signaling

The DNA Damage Response: Ten Years After

Harper, J. W., & Elledge, S. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.015 · Cited by 1,705

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

Interaction of the Fanconi Anemia Proteins and BRCA1 in a Common Pathway

Garcia-Higuera, I., Taniguchi, T., Ganesan, S., Meyn, M. S., Timmers, C., Hejna, J., Grompe, M., & D'Andrea, A. D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00173-3 · Cited by 1,198

Ubiquitin signalling in the NF-κB pathway

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

Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.

Bienko, M., Green, C. M., Crosetto, N., Rudolf, F., Zapart, G., Coull, B., Kannouche, P., Wider, G., Peter, M., Lehmann, A. R., et al. (2005) · Science · doi:10.1126/science.1120615 · Cited by 712

Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins

Wang, W. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2159 · Cited by 663

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

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

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

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

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764

Tlr signalling augments macrophage bactericidal activity through mitochondrial ros

West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960

The emerging complexity of protein ubiquitination

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

The role of ubiquitination in tumorigenesis and targeted drug discovery

Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744

Structural insights into the catalysis and regulation of E3 ubiquitin ligases

Buetow, L., & Huang, D. T. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.91 · Cited by 679

OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis

Mevissen, T. E. T., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., El Oualid, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.046 · 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

Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets

Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563

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

The ubiquitin-modifying enzyme A20 restricts ubiquitination of the kinase RIPK3 and protects cells from necroptosis

Onizawa, M., Oshima, S., Schulze-Topphoff, U., Oses-Prieto, J. A., Lu, T., Tavares, R., Prodhomme, T., Duong, B., Whang, M. I., Advincula, R., et al. (2015) · Nature Immunology · doi:10.1038/ni.3172 · Cited by 284

Regulation of NF-κB by ubiquitination

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

A nuclear poly(ADP-Ribose)-dependent signalosome confers DNA damage-induced IκB kinase activation.

Stilmann, M., Hinz, M., Arslan, S. Ç., Zimmer, A., Schreiber, V., & Scheidereit, C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.032 · Cited by 232

Ubiquitin in the immune system

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

Act1, a U-box E3 Ubiquitin Ligase for IL-17 Signaling

Liu, C., Qian, W., Qian, Y., Giltiay, N. V., Lu, Y., Swaidani, S., Misra, S., Deng, L., Chen, Z. J., & Li, X. (2009) · Science Signaling · doi:10.1126/scisignal.2000382 · Cited by 224

Allosteric post-translational modification codes

Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211

Unanchored K48-Linked Polyubiquitin Synthesized by the E3-Ubiquitin Ligase TRIM6 Stimulates the Interferon-IKKε Kinase-Mediated Antiviral Response

Rajsbaum, R., Versteeg, G. A., Schmid, S., Maestre, A. M., Belicha-Villanueva, A., Martínez-Romero, C., Patel, J. R., Morrison, J., Pisanelli, G., Miorin, L., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.04.018 · Cited by 168

Modulation of Phototropic Responsiveness in Arabidopsis through Ubiquitination of Phototropin 1 by the CUL3-Ring E3 Ubiquitin Ligase CRL3NPH3

Roberts, D., Pedmale, U. V., Morrow, J., Sachdev, S., Lechner, E., Tang, X., Zheng, N., Hannink, M., Genschik, P., & Liscum, E. (2011) · The Plant Cell · doi:10.1105/tpc.111.087999 · Cited by 150

New knowledge on critical osteoclast formation and activation pathways from study of rare genetic diseases of osteoclasts: focus on the RANK/RANKL axis

Crockett, J. C., Mellis, D. J., Scott, D. I., & Helfrich, M. H. (2011) · Osteoporosis International · doi:10.1007/s00198-010-1272-8 · Cited by 143

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

Ligandability of E3 Ligases for Targeted Protein Degradation Applications

Belcher, B. P., Ward, C. C., & Nomura, D. K. (2023) · Biochemistry · doi:10.1021/acs.biochem.1c00464 · Cited by 132

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

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

Systems‐wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation

Satpathy, S., Wagner, S. A., Beli, P., Gupta, R., Kristiansen, T. A., Malinova, D., Francavilla, C., Tolar, P., Bishop, G. A., Hostager, B. S., et al. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145880 · Cited by 124

HuR is required for IL-17-induced Act1-mediated CXCL1 and CXCL5 mRNA stabilization

Herjan, T., Yao, P., Qian, W., Li, X., Liu, C., Bulek, K., Sun, D., Yang, W.-P., Zhu, J., He, A., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1203315 · Cited by 95

Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescence-based multiplex assay format.

Tian, X., Isamiddinova, N. S., Peroutka, R. J., Goldenberg, S. J., Mattern, M. R., Nicholson, B., & Leach, C. (2011) · ASSAY and Drug Development Technologies · doi:10.1089/adt.2010.0317 · Cited by 76

NF-κB and Extrinsic Cell Death Pathways – Entwined Do-or-Die Decisions for T cells

Blanchett, S., Boal-Carvalho, I., Layzell, S., & Seddon, B. (2021) · Trends in Immunology · doi:10.1016/j.it.2020.10.013 · Cited by 58

The 26S proteasome and initiation of gene transcription.

Durairaj, G., & Kaiser, P. (2014) · Biomolecules · doi:10.3390/biom4030827 · Cited by 34

Overexpression of SphK2 contributes to ATRA resistance in colon cancer through rapid degradation of cytoplasmic RXRα by K48/K63-linked polyubiquitination

Shi, W.-N., Cui, S.-X., Song, Z.-Y., Wang, S.-Q., Sun, S.-Y., Yu, X.-F., Li, Y., Zhang, Y.-H., Gao, Z.-H., & Qu, X.-J. (2017) · Oncotarget · doi:10.18632/oncotarget.17174 · Cited by 24

Unraveling motion in proteins by combining NMR relaxometry and molecular dynamics simulations: A case study on ubiquitin

Champion, C., Lehner, M., Smith, A. A., Ferrage, F., Bolik-Coulon, N., & Riniker, S. (2024) · The Journal of Chemical Physics · doi:10.1063/5.0188416 · Cited by 11

A ubiquitin‐binding CUE domain in presenilin‐1 enables interaction with K63‐linked polyubiquitin chains

Duggan, S. P., Yan, R., & McCarthy, J. V. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.03.008 · Cited by 10

The ESCRT-deubiquitinating enzyme USP8 in the cervical spinal cord of wild-type and Vps54-recessive (wobbler) mutant mice

Paiardi, C., Pasini, M. E., Amadeo, A., Gioria, M., & Berruti, G. (2014) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1096-7 · Cited by 9