The increasing complexity of the ubiquitin code
Abstract
Ubiquitylation is essential for signal transduction as well as cell division and differentiation in all eukaryotes. Substrate modifications range from a single ubiquitin molecule to complex polymeric chains, with different types of ubiquitylation often eliciting distinct outcomes. The recent identification of novel chain topologies has improved our understanding of how ubiquitylation establishes precise communication within cells. Here, we discuss how the increasing complexity of ubiquitylation is employed to ensure robust and faithful signal transduction in eukaryotic cells.
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More than 600 E3 ligases in the human genome fall into different classes depending on which ubiquitin ligation strategy they use.
“the more than 600 E3 ligases in the human genome fall into different classes, depending on which ubiquitin ligation strategy they use (reviewed in refs80,108–110).”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [108]
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works
Self-citationPINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · 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
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,387 · see citing works
Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer
Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.11.025 · Cited by 2,317 · see citing works
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202 · see citing works
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125 · see citing works
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872 · 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
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,718 · see citing works
TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
Gack, M. U., Shin, Y. C., Joo, C.-H., Urano, T., Liang, C., Sun, L., Takeuchi, O., Akira, S., Chen, Z. J., Inoue, S., et al. (2007) · Nature · doi:10.1038/nature05732 · Cited by 1,683 · see citing works
A proteomics approach to understanding protein ubiquitination
Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D. J., & Gygi, S. P. (2003) · Nature Biotechnology · doi:10.1038/nbt849 · Cited by 1,601 · see citing works
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,582 · 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
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
TRAF6 is a signal transducer for interleukin-1
Cao, Z., Xiong, J., Takeuchi, M., Kurama, T., & Goeddel, D. V. (1996) · Nature · doi:10.1038/383443a0 · Cited by 1,305 · see citing works
Phosphorylation of the Autophagy Receptor Optineurin Restricts <i>Salmonella</i> Growth
Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., et al. (2011) · Science · doi:10.1126/science.1205405 · Cited by 1,298 · see citing works
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · see citing works
Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, A. J., Hochstrasser, M., Finley, D. J., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,125 · see citing works
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,056 · see citing works
Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Sarraf, S. A., Raman, M., Guarani, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,020 · 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
Self-citationPARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease
Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953 · see citing works
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
Schulman, B. A., & Harper, J. W. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2673 · Cited by 944 · 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
Doil, C., Mailand, N., Bekker‐Jensen, S., Ménard, P., Larsen, D. H., Pepperkok, R., Ellenberg, J., Panier, S., Durocher, D., Bártek, J., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.041 · Cited by 938 · see citing works
Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906 · see citing works
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
Tatham, M. H., Geoffroy, M., Shen, L., Plechanovová, A., Hattersley, N., Jaffray, E., Palvimo, J. J., & Hay, R. T. (2008) · Nature Cell Biology · doi:10.1038/ncb1716 · Cited by 837 · see citing works
A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal
Johnson, E. S., Philip, C. M., Ota, I. M., & Varshavsky, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17442 · Cited by 816 · see citing works
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806 · 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
The RIDDLE Syndrome Protein Mediates a Ubiquitin-Dependent Signaling Cascade at Sites of DNA Damage
Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A., Kolas, N. K., Miller, E. S., Nakada, S., Ylanko, J., Olivarius, S., Mendez, M., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.042 · Cited by 757 · see citing works
Ubiquitin-Binding Proteins: Decoders of Ubiquitin-Mediated Cellular Functions
Husnjak, K., & Đikić, I. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051810-094654 · Cited by 755 · 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
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
Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway
Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Pérès, L., Zhou, J., Zhu, J., Raught, B., & de Thé, H. (2008) · Nature Cell Biology · doi:10.1038/ncb1717 · Cited by 726 · see citing works
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 · see citing works
Ordureau, A., Sarraf, S. A., Duda, D. M., Heo, J., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.007 · Cited by 693 · see citing works
PINK1 is degraded through the N-end rule pathway
Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628 · see citing works
Mevissen, T. E. T., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., Oualid, F. E., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.046 · Cited by 621 · see citing works
Zeng, W., Sun, L., Jiang, X., Chen, X., Hou, F., Adhikari, A., Xu, M., & Chen, Z. J. (2010) · Cell · doi:10.1016/j.cell.2010.03.029 · Cited by 613 · 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
Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
Swaney, D. L., Beltrão, P., Starita, L. M., Guo, A., Rush, A. J., Fields, S., Krogan, N. J., & Villén, J. (2013) · Nature Methods · doi:10.1038/nmeth.2519 · Cited by 601 · 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
Direct activation of protein kinases by unanchored polyubiquitin chains
Xia, Z.-P., Sun, L., Chen, X., Pineda, G., Jiang, X., Adhikari, A., Zeng, W., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature08247 · Cited by 570 · see citing works
Ubiquitin Chain Editing Revealed by Polyubiquitin Linkage-Specific Antibodies
Newton, K., Matsumoto, M. L., Wertz, I. E., Kirkpatrick, D. S., Lill, J. R., Tan, J., Dugger, D. L., Gordon, N. C., Sidhu, S. S., Fellouse, F. A., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.039 · Cited by 553 · see citing works
A Ubiquitin Mutant with Specific Defects in DNA Repair and Multiubiquitination
Spence, J. L., Sadis, S., Haas, A. L., & Finley, D. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1265 · Cited by 550 · see citing works
Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex
Jin, L., Williamson, A. P., Banerjee, S., Philipp, I., & Rapé, M. (2008) · Cell · doi:10.1016/j.cell.2008.04.012 · Cited by 536 · see citing works
Richly, H., Rapé, M., Braun, S. J., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523 · see citing works
FAM/USP9x, a Deubiquitinating Enzyme Essential for TGFβ Signaling, Controls Smad4 Monoubiquitination
Dupont, S., Mamidi, A., Cordenonsi, M., Montagner, M., Zacchigna, L., Adorno, M., Martello, G., Stinchfield, M. J., Soligo, S., Morsut, L., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.051 · Cited by 494 · 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
Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair
Psakhye, I., & Jentsch, S. (2012) · Cell · doi:10.1016/j.cell.2012.10.021 · Cited by 484 · see citing works
Mechanism of phospho-ubiquitin-induced PARKIN activation
Wauer, T., Šimíček, M., Schubert, A. F., & Komander, D. (2015) · Nature · doi:10.1038/nature14879 · Cited by 479 · see citing works
Enhanced Protein Degradation by Branched Ubiquitin Chains
Meyer, H., & Rapé, M. (2014) · Cell · doi:10.1016/j.cell.2014.03.037 · Cited by 466 · see citing works
Kim, H. T., Kim, K. P., Lledı́as, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., Gygi, S. P., & Goldberg, A. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609659200 · Cited by 438 · 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
Global Identification of Modular Cullin-RING Ligase Substrates
Emanuele, M. J., Elia, A. E. H., Xu, Q., Thoma, C. R., Izhar, L., Leng, Y., Guo, A., Chen, Y., Rush, A. J., Hsu, P. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.019 · Cited by 403 · see citing works
K11-Linked Polyubiquitination in Cell Cycle Control Revealed by a K11 Linkage-Specific Antibody
Matsumoto, M. L., Wickliffe, K. E., Dong, K. C., Yu, C., Bosanac, I., Bustos, D. J., Phu, L., Kirkpatrick, D. S., Hymowitz, S. G., Rapé, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.001 · Cited by 401 · 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
Cell Cycle–Regulated Modification of the Ribosome by a Variant Multiubiquitin Chain
Spence, J. L., Gali, R. R., Dittmar, G. A. G., Sherman, F., Karin, M., & Finley, D. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00011-8 · Cited by 378 · see citing works
USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin
Durcan, T. M., Tang, M. Y., Pérusse, J. R., Dashti, E. A., Aguileta, M. A., McLelland, G., Gros, P., Shaler, T. A., Faubert, D., Coulombe, B., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201489729 · Cited by 375 · see citing works
AMSH is an endosome-associated ubiquitin isopeptidase
McCullough, J., Clague, M. J., & Urbé, S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401141 · Cited by 369 · see citing works
TRIP12 and UBR5 Suppress Spreading of Chromatin Ubiquitylation at Damaged Chromosomes
Guðjόnsson, Þ., Altmeyer, M., Savic, V., Toledo, L. I., Dinant, C., Grøfte, M., Bártková, J., Poulsen, M., Oka, Y., Bekker‐Jensen, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.039 · Cited by 338 · see citing works
SUMO‐targeted ubiquitin ligases in genome stability
Prudden, J., Kaeser-Pebernard, S., Raffa, G. D., Slavin, D. A., Perry, J. J. P., Tainer, J. A., McGowan, C. H., & Boddy, M. N. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601838 · Cited by 334 · see citing works
Ubiquitin-dependent regulation of COPII coat size and function
Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Baumgärtel, C., Schekman, R., & Rape, M. (2012) · Nature · doi:10.1038/nature10822 · Cited by 330 · see citing works
USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria
Cunningham, C. N., Baughman, J. M., Phu, L., Tea, J. S., Yu, C., Coons, M. M., Kirkpatrick, D. S., Bingol, B., & Corn, J. E. (2015) · Nature Cell Biology · doi:10.1038/ncb3097 · Cited by 329 · see citing works
Bremm, A., Freund, S. M. V., & Komander, D. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1873 · Cited by 324 · see citing works
Ubiquitin-dependent Proteolytic Control of SUMO Conjugates
Uzunova, K., Göttsche, K., Miteva, M., Weisshaar, S. R., Glanemann, C., Schnellhardt, M., Niessen, M. T., Scheel, H., Hofmann, K., Johnson, E. S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706505200 · Cited by 314 · see citing works
RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair
Galanty, Y., Belotserkovskaya, R., Coates, J., & Jackson, S. P. (2012) · Genes & Development · doi:10.1101/gad.188284.112 · Cited by 314 · see citing works
Ordureau, A., Heo, J.-M., Duda, D. M., Paulo, J. A., Olszewski, J. L., Yanishevski, D., Rinehart, J., Schulman, B. A., & Harper, J. W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506593112 · Cited by 310 · see citing works
Crosas, B., Hanna, J. W., Kirkpatrick, D. S., Zhang, D. P., Tone, Y., Hathaway, N. A., Buecker, C., Leggett, D., Schmidt, M., King, R. W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.051 · Cited by 305 · see citing works
Petroski, M. D., & Deshaies, R. J. (2005) · Cell · doi:10.1016/j.cell.2005.09.033 · Cited by 304 · see citing works
Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis
Wauer, T., Swatek, K. N., Wagstaff, J. L., Gladkova, C., Pruneda, J. N., Michel, M. A., Gersch, M., Johnson, C. M., Freund, S. M. V., & Komander, D. (2014) · The EMBO Journal · doi:10.15252/embj.201489847 · Cited by 303 · see citing works
Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
Virdee, S., Ye, Y., Nguyen, D., Komander, D., & Chin, J. W. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.426 · Cited by 296 · see citing works
Molecular Insights into Polyubiquitin Chain Assembly
VanDemark, A. P., Hofmann, R. M., Tsui, C., Pickart, C. M., & Wolberger, C. (2001) · Cell · doi:10.1016/s0092-8674(01)00387-7 · Cited by 293 · see citing works
Identification of a physiological E2 module for the human anaphase-promoting complex
Williamson, A. P., Wickliffe, K. E., Mellone, B. G., Song, L., Karpen, G. H., & Rapé, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907887106 · Cited by 290 · 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
Lauwers, E., Jacob, C., & André, B. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810114 · Cited by 275 · see citing works
Lysine 63‐linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh‐e, A., & Tanaka, K. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.305 · Cited by 260 · see citing works
Conformational switching of the 26S proteasome enables substrate degradation
Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251 · see citing works
UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit
Garnett, M. J., Mansfeld, J., Godwin, C., Matsusaka, T., Wu, J., Russell, P., Pines, J., & Venkitaraman, A. R. (2009) · Nature Cell Biology · doi:10.1038/ncb1983 · Cited by 248 · see citing works
Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation
Wertz, I. E., Newton, K., Seshasayee, D., Kusam, S., Lam, C., Zhang, J., Popovych, N., Helgason, E., Schoeffler, A. J., Jeet, S., et al. (2015) · Nature · doi:10.1038/nature16165 · Cited by 248 · see citing works
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
UBE2S drives elongation of K11-linked ubiquitin chains by the Anaphase-Promoting Complex
Wu, T., Merbl, Y., Huo, Y., Gallop, J. L., Tzur, A., & Kirschner, M. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912802107 · Cited by 240 · see citing works
A two-step mechanism for TRF2-mediated chromosome-end protection
Okamoto, K., Bartocci, C., Ouzounov, I., Diedrich, J. K., Yates, J. R., & Denchi, E. L. (2013) · Nature · doi:10.1038/nature11873 · Cited by 240 · see citing works
Kim, N. C., Tresse, E., Kolaitis, R., Molliex, A., Thomas, R. E., Alami, N. H., Wang, B., Joshi, A., Smith, R. B., Ritson, G. P., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.029 · Cited by 240 · see citing works
SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
Yin, Y., Seifert, A., Chua, J. S., Maure, J.-F., Golebiowski, F., & Hay, R. T. (2012) · Genes & Development · doi:10.1101/gad.189274.112 · Cited by 237 · see citing works
Expanding the ubiquitin code through post‐translational modification
Herhaus, L., & Đikić, I. (2015) · EMBO Reports · doi:10.15252/embr.201540891 · Cited by 230 · see citing works
Baboshina, O. V., & Haas, A. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2823 · Cited by 226 · see citing works
Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., & Cohen, R. E. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.27 · Cited by 223 · see citing works
Ernst, R., Mueller, B., Ploegh, H. L., & Schlieker, C. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.016 · Cited by 222 · see citing works
RNF168 Promotes Noncanonical K27 Ubiquitination to Signal DNA Damage
Gatti, M., Pinato, S., Maiolica, A., Rocchio, F., Prato, M. G., Aebersold, R. H., & Penengo, L. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.021 · Cited by 220 · see citing works
Substrate degradation by the proteasome: A single-molecule kinetic analysis
Lu, Y., Lee, B., King, R. W., Finley, D. J., & Kirschner, M. W. (2015) · Science · doi:10.1126/science.1250834 · Cited by 218 · see citing works
Song, E. J., Werner, S. L., Neubauer, J., Stegmeier, F. P., Aspden, J. L., Rio, D. C., Harper, J. W., Elledge, S. J., Kirschner, M. W., & Rapé, M. (2010) · Genes & Development · doi:10.1101/gad.1925010 · Cited by 216 · see citing works
Assembly and Specific Recognition of K29- and K33-Linked Polyubiquitin
Michel, M. A., Elliott, P. R., Swatek, K. N., Šimíček, M., Pruneda, J. N., Wagstaff, J. L., Freund, S. M. V., & Komander, D. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.042 · Cited by 215 · see citing works
The Yeast Hex3·Slx8 Heterodimer Is a Ubiquitin Ligase Stimulated by Substrate Sumoylation
Xie, Y., Kerscher, O., Kroetz, M. B., McConchie, H. F., Sung, P., & Hochstrasser, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706025200 · Cited by 213 · see citing works
Chen, B., Mariano, J. M., Tsai, Y. C., Chan, A. H., Cohen, M. M., & Weissman, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506618103 · Cited by 213 · see citing works
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
Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family
Cui, J., Yao, Q., Li, S., Ding, X., Lu, Q., Mao, H., Liu, L., Zheng, N., Chen, S., & Shao, F. (2010) · Science · doi:10.1126/science.1193844 · Cited by 203 · see citing works
RNF26 Temporally Regulates Virus-Triggered Type I Interferon Induction by Two Distinct Mechanisms
Qin, Y., Zhou, M., Hu, M., Hu, Y.-H., Zhang, J., Guo, L., Zhong, B., & Shu, H. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004358 · Cited by 203 · see citing works
K63 polyubiquitination is a new modulator of the oxidative stress response
Silva, G. M., Finley, D. J., & Vogel, C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2955 · Cited by 199 · see citing works
Deubiquitylase OTUD3 regulates PTEN stability and suppresses tumorigenesis
Yuan, L., Lv, Y., Li, H., Gao, H., Song, S., Zhang, Y., Xing, G., Kong, X., Wang, L., Li, Y., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3218 · Cited by 199 · see citing works
Ubiquitin chain conformation regulates recognition and activity of interacting proteins
Ye, Y., Blaser, G., Horrocks, M. H., Ruedas-Rama, M. J., Ibrahim, S., Zhukov, A. A., Orte, Á., Klenerman, D., Jackson, S., & Komander, D. (2012) · Nature · doi:10.1038/nature11722 · Cited by 191 · see citing works
Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming
Maspero, E., Valentini, E., Mari, S., Cecatiello, V., Soffientini, P., Pasqualato, S., & Polo, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2566 · Cited by 188 · see citing works
Molecular Basis and Regulation of OTULIN-LUBAC Interaction
Elliott, P. R., Nielsen, S. V., Marco‐Casanova, P., Fiil, B. K., Keusekotten, K., Mailand, N., Freund, S. M. V., Gyrd‐Hansen, M., & Komander, D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.018 · Cited by 185 · see citing works
Cell-fate determination by ubiquitin-dependent regulation of translation
Werner, A., Iwasaki, S., McGourty, C. A., Medina-Ruiz, S., Teerikorpi, N., Fedrigo, I., Ingolia, N. T., & Rape, M. (2015) · Nature · doi:10.1038/nature14978 · Cited by 184 · see citing works
Self-citationYuan, W.-C., Lee, Y.-R., Lin, S., Chang, L.-Y., Tan, Y. P., Hung, C., Kuo, J., Liu, C., Lin, M.-Y., Xu, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.035 · Cited by 182 · see citing works
Identification of a novel ubiquitin-conjugating enzyme involved in mitotic cyclin degradation
Yu, H., King, R. W., Peters, J., & Kirschner, M. W. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00513-4 · Cited by 180 · see citing works
Binding of OTULIN to the PUB Domain of HOIP Controls NF-κB Signaling
Schaeffer, V., Akutsu, M., Olma, M. H., Gomes, L. C., Kawasaki, M., & Đikić, I. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.016 · Cited by 179 · see citing works
Shabek, N., Herman-Bachinsky, Y., Buchsbaum, S., Lewinson, O., Haj‐Yahya, M., Hejjaoui, M., Lashuel, H. A., Sommer, T., Brik, A., & Ciechanover, A. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.011 · Cited by 168 · see citing works
Kristariyanto, Y. A., Rehman, S. A. A., Campbell, D. G., Morrice, N. A., Johnson, C., Toth, R. L., & Kulathu, Y. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.041 · Cited by 160 · see citing works
van Wijk, S. J. L., Fiškin, E., Putyrski, M., Pampaloni, F., Hou, J., Wild, P. S., Kensche, T., Grecco, H. E., Bastiaens, P. I. H., & Đikić, I. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.017 · Cited by 155 · see citing works
Liu, J., Han, C., Xie, B., Wu, Y., Liu, S., Chen, K., Meng, X., Zhang, Y., Song, L., Li, Z., et al. (2014) · Nature Immunology · doi:10.1038/ni.2898 · Cited by 148 · see citing works
Ubiquitin acetylation inhibits polyubiquitin chain elongation
Ohtake, F., Saeki, Y., Sakamoto, K., Ohtake, K., Nishikawa, H., Tsuchiya, H., Ohta, T., Tanaka, K., & Kanno, J. (2014) · EMBO Reports · doi:10.15252/embr.201439152 · Cited by 148 · see citing works
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
Hwang, C., Shemorry, A., Auerbach, D., & Varshavsky, A. J. (2010) · Nature Cell Biology · doi:10.1038/ncb2121 · Cited by 147 · see citing works
APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1
Dimova, N. V., Hathaway, N. A., Lee, B., Kirkpatrick, D. S., Berkowitz, M. L., Gygi, S. P., Finley, D. J., & King, R. W. (2012) · Nature Cell Biology · doi:10.1038/ncb2425 · Cited by 146 · see citing works
Assembly, analysis and architecture of atypical ubiquitin chains
Hospenthal, M. K., Freund, S. M. V., & Komander, D. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2547 · Cited by 146 · see citing works
Lysine 63-linked polyubiquitination is required for EGF receptor degradation
Huang, F., Zeng, X.-M., Kim, W., Balasubramani, M., Fortian, A., Gygi, S., Yates, N., & Sorkin, A. (2013) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1308014110 · Cited by 141 · see citing works
Regulated Degradation of Spindle Assembly Factors by the Anaphase-Promoting Complex
Song, L., & Rapé, M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.038 · Cited by 133 · see citing works
Deubiquitinase DUBA is a post-translational brake on interleukin-17 production in T cells
Rutz, S., Kayagaki, N., Phung, Q. T., Eidenschenk, C., Noubade, R., Wang, X., Lesch, J., Lu, R. O., Newton, K., Huang, O. W., et al. (2014) · Nature · doi:10.1038/nature13979 · Cited by 129 · see citing works
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
Engineering and Structural Characterization of a Linear Polyubiquitin-Specific Antibody
Matsumoto, M. L., Dong, K. C., Yu, C., Phu, L., Gao, X., Hannoush, R. N., Hymowitz, S. G., Kirkpatrick, D. S., Dixit, V. M., & Kelley, R. F. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.053 · Cited by 123 · see citing works
Degradation signals in the lysine–asparagine sequence space
Suzuki, T., & Varshavsky, A. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6017 · Cited by 117 · see citing works
Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains
Branigan, E., Plechanovová, A., Jaffray, E., Naismith, J. H., & Hay, R. T. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3052 · Cited by 116 · see citing works
Gibbs‐Seymour, I., Oka, Y., Rajendra, E., Weinert, B. T., Passmore, L. A., Patel, K. J., Olsen, J. V., Choudhary, C., Bekker‐Jensen, S., & Mailand, N. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.12.001 · Cited by 116 · see citing works
Presence of protein A24 in rat liver nucleosomes.
Goldknopf, I. L., French, M. F., Musso, R. E., & Busch, H. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5492 · Cited by 109 · see citing works
Regulation of Ubiquitin Chain Initiation to Control the Timing of Substrate Degradation
Williamson, A. P., Banerjee, S., Zhu, X., Philipp, I., Iavarone, A. T., & Rapé, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.022 · Cited by 100 · see citing works
Mixed-Linkage Ubiquitin Chains Send Mixed Messages
Nakasone, M. A., Livnat‐Levanon, N., Glickman, M. H., Cohen, R. E., & Fushman, D. (2013) · Structure · doi:10.1016/j.str.2013.02.019 · Cited by 100 · see citing works
A ubiquitin-interacting motif protects polyubiquitinated Met4 from degradation by the 26S proteasome
Flick, K. M., Raasi, S., Zhang, H., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1402 · Cited by 99 · see citing works
Cezanne (OTUD7B) regulates HIF‐1α homeostasis in a proteasome‐independent manner
Bremm, A., Moniz, S., Mader, J. K., Rocha, S., & Komander, D. (2014) · EMBO Reports · doi:10.15252/embr.201438850 · Cited by 97 · see citing works
Brown, N. G., VanderLinden, R. T., Watson, E. R., Qiao, R., Grace, C. R., Yamaguchi, M., Weissmann, F., Frye, J. J., Dube, P., Cho, S. E., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504161112 · Cited by 97 · see citing works
Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase
Wang, M., Cheng, D., Peng, J., & Pickart, C. M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601061 · Cited by 92 · see citing works
Swaney, D. L., Rodríguez‐Mias, R. A., & Villén, J. (2015) · EMBO Reports · doi:10.15252/embr.201540298 · Cited by 91 · see citing works
The Proteasome Distinguishes between Heterotypic and Homotypic Lysine-11-Linked Polyubiquitin Chains
Grice, G. L., Lobb, I., Weekes, M. P., Gygi, S. P., Antrobus, R., & Nathan, J. A. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.061 · Cited by 90 · see citing works
Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains
Valkevich, E. M., Sanchez, N. A., Ge, Y., & Strieter, E. R. (2014) · Biochemistry · doi:10.1021/bi5006305 · Cited by 89 · see citing works
Tsuchiya, H., Tanaka, K., & Saeki, Y. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.05.080 · Cited by 72 · see citing works
Unique Structural, Dynamical, and Functional Properties of K11-Linked Polyubiquitin Chains
Castañeda, C. A., Kashyap, T. R., Nakasone, M. A., Krueger, S., & Fushman, D. (2013) · Structure · doi:10.1016/j.str.2013.04.029 · Cited by 63 · see citing works
Min, M., Mevissen, T. E. T., Luca, M. D., et al. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-02-0102 · 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
Locke, M., Toth, J. I., & Petroski, M. D. (2014) · Biochemical Journal · doi:10.1042/bj20120662 · Cited by 60 · see citing works
Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage
Saeki, Y., Tayama, Y., Toh‐e, A., & Yokosawa, H. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.216 · Cited by 58 · see citing works
Ter94 ATPase Complex Targets K11-Linked Ubiquitinated Ci to Proteasomes for Partial Degradation
Zhang, Z., Lv, X., Yin, W.-C., Zhang, X., Feng, J., Wu, W., Hui, C., Zhang, L., & Zhao, Y. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.006 · Cited by 46 · see citing works
Microtubule-Dependent Regulation of Mitotic Protein Degradation
Song, L., Craney, A., & Rapé, M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.022 · Cited by 36 · see citing works
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Hyer, M. L., Milhollen, M. A., Ciavarri, J., Fleming, P., Traore, T., Sappal, D., Huck, J., Shi, J., Gavin, J., Brownell, J., et al. (2018) · Nature Medicine · doi:10.1038/nm.4474 · Cited by 447 · see citing works
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works
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Oh, E., Akopian, D., & Rape, M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062802 · Cited by 339 · see citing works
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Schneider, M., Radoux, C. J., Hercules, A., Ochoa, D., Dunham, I., Zalmas, L.-P., Hessler, G., Ruf, S., Shanmugasundaram, V., Hann, M. M., et al. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00245-x · Cited by 273 · see citing works
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Gavory, G., O'Dowd, C. R., Helm, M. D., Flasz, J., Arkoudis, E., Dossang, A., Hughes, C., Cassidy, E., McClelland, K., Odrzywol, E., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2528 · Cited by 224 · see citing works
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Belcher, B. P., Ward, C. C., & Nomura, D. K. (2023) · Biochemistry · doi:10.1021/acs.biochem.1c00464 · Cited by 132 · see citing works
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O’Connor, H. F., & Huibregtse, J. M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2529-6 · Cited by 42 · see citing works
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Biswas, K., Philip, S., Yadav, A., Martin, B. K., Burkett, S., Singh, V., Babbar, A., North, S. L., Chang, S., & Sharan, S. K. (2018) · Nature Communications · doi:10.1038/s41467-018-03020-6 · Cited by 41 · see citing works
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Gyrd-Hansen, M. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.93 · Cited by 15 · see citing works
- Authors
- Yau, R., & Rape, M.
- Affiliations
- Howard Hughes Medical Institute (US)
- ORCID
- Yau, Richard
- Venue
- Nature Cell Biology
- Published
- 2016-05-27
- Volume
- 18
- Issue
- 6
- Pages
- 579-586
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2398731353
- Cited by
- 1,054
- References
- 151
- Citations by year
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- FWCI
- 9.11
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- ubiquitination, polyubiquitin chains, signal transduction, protein modification, cell division, cell differentiation
- MeSH terms
- Animals, Humans, Models, Molecular, Signal Transduction, Ubiquitin, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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