Principles of Ubiquitin-Dependent Signaling

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing

Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775

PINK1 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

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

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

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 2,416

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

Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain

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

Role of histone H2A ubiquitination in Polycomb silencing

Wang, H., Wang, L., Erdjument‐Bromage, H., Vidal, M., Tempst, P., Jones, R. S., & Zhang, Y. (2004) · Nature · doi:10.1038/nature02985 · Cited by 1,856

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 1,643

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

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523

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

Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella 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

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

HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.

Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234

RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins

Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,193

Mechanisms of Deubiquitinase Specificity and Regulation

Mevissen, T. E. T., & Komander, D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044916 · Cited by 1,069

RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly

Huen, M. S. Y., Grant, R. A., Manke, I. A., Minn, K. T., Yu, X., Yaffe, M. B., & Chen, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.041 · Cited by 1,068

The increasing complexity of the ubiquitin code

Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054

Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization

Sarraf, S. A., Raman, M., Guarani-Pereira, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,010

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Connell, P. M., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., & Patterson, C. (2000) · Nature Cell Biology · doi:10.1038/35050618 · Cited by 1,002

RNF168 Binds and Amplifies Ubiquitin Conjugates on Damaged Chromosomes to Allow Accumulation of Repair Proteins

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 981

Involvement of linear polyubiquitylation of NEMO in NF-κB activation

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

The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation

Welcker, M., Orian, A., Jin, J., Grim, J. A., Harper, J. W., Eisenman, R. N., & Clurman, B. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402770101 · Cited by 942

Deubiquitylating enzymes and drug discovery: emerging opportunities

Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940

Orchestration of the DNA-Damage Response by the RNF8 Ubiquitin Ligase

Kolas, N. K., Chapman, J. R., Nakada, S., Ylanko, J., Chahwan, R., Sweeney, F. D., Panier, S., Mendez, M., Wildenhain, J., Thomson, T. M., et al. (2007) · Science · doi:10.1126/science.1150034 · Cited by 932

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

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

Role of Bmi-1 and Ring1A in H2A Ubiquitylation and Hox Gene Silencing

Cao, R., Tsukada, Y.-I., & Zhang, Y. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.12.002 · Cited by 880

c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptorPreprint

Levkowitz, G., Waterman, H., Zamir, E., Kam, Z., Oved, S., Langdon, W. Y., Beguinot, L., Geiger, B., & Yarden, Y. (1998) · Genes & Development · doi:10.1101/gad.12.23.3663 · Cited by 865

PCGF Homologs, CBX Proteins, and RYBP Define Functionally Distinct PRC1 Family Complexes

Gao, Z., Zhang, J., Bonasio, R., Strino, F., Sawai, A., Parisi, F., Kluger, Y., & Reinberg, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.002 · Cited by 852

LXR Regulates Cholesterol Uptake Through Idol-Dependent Ubiquitination of the LDL Receptor

Zelcer, N., Hong, C., Boyadjian, R., & Tontonoz, P. (2009) · Science · doi:10.1126/science.1168974 · Cited by 848

Encoding and Decoding Cellular Information through Signaling Dynamics

Purvis, J. E., & Lahav, G. (2013) · Cell · doi:10.1016/j.cell.2013.02.005 · Cited by 820

Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB

Scheuermann, J. C., Alonso, A. G. D. A., Oktaba, K., Ly‐Hartig, N., McGinty, R. K., Fraterman, S., Wilm, M. S., Muir, T. W., & Müller, J. (2010) · Nature · doi:10.1038/nature08966 · Cited by 816

Phosphorylation‐dependent degradation of c‐Myc is mediated by the F‐box protein Fbw7

Yada, M., Hatakeyama, S., Kamura, T., Nishiyama, M., Tsunematsu, R., Imaki, H., Ishida, N., Okumura, F., Nakayama, K., & Nakayama, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600217 · Cited by 810

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

Autophagy in the Cellular Energetic Balance

Singh, R., & Cuervo, A. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.004 · Cited by 788

Variant PRC1 Complex-Dependent H2A Ubiquitylation Drives PRC2 Recruitment and Polycomb Domain Formation

Blackledge, N. P., Farcas, A. M., Kondo, T., King, H. W., McGouran, J. F., Hanssen, L. L. P., Ito, S., Cooper, S., Kondo, K., Koseki, Y., et al. (2014) · Cell · doi:10.1016/j.cell.2014.05.004 · Cited by 778

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

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

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

Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis

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 718

Histone H2B Monoubiquitination Functions Cooperatively with FACT to Regulate Elongation by RNA Polymerase II

Pavri, R., Zhu, B., Li, G., Trojer, P., Mandal, S. S., Shilatifard, A., & Reinberg, D. (2006) · Cell · doi:10.1016/j.cell.2006.04.029 · Cited by 708

Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response

Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., & Elledge, S. J. (2007) · Science · doi:10.1126/science.1139476 · Cited by 695

PINK1 is degraded through the N-end rule pathway

Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 694

RNF168 Ubiquitinates K13-15 on H2A/H2AX to Drive DNA Damage Signaling

Mattiroli, F., Vissers, J. H. A., van Dijk, W. J., Ikpa, P. T., Citterio, E., Vermeulen, W., Marteijn, J. A. F., & Sixma, T. K. (2012) · Cell · doi:10.1016/j.cell.2012.08.005 · Cited by 688

53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark

Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686

Building and decoding ubiquitin chains for mitophagy

Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 685

RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites

Sobhian, B., Shao, G., Lilli, D. R., Culhane, A. C., Moreau, L. A., Xia, B., Livingston, D. M., & Greenberg, R. A. (2007) · Science · doi:10.1126/science.1139516 · Cited by 672

Mechanisms and function of substrate recruitment by F-box proteins

Skaar, J. R., Pagan, J. K., & Pagano, M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3582 · Cited by 671

A Ribosome-Bound Quality Control Complex Triggers Degradation of Nascent Peptides and Signals Translation Stress

Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A. G., Williams, C. C., Li, G., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 650

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 621

REV7 counteracts DNA double-strand break resection and affects PARP inhibition

Xu, G., Chapman, J. R., Brandsma, I., Yuan, J., Mistrík, M., Bouwman, P., Bártková, J., Gogola, E., Warmerdam, D. O., Barazas, M., et al. (2015) · Nature · doi:10.1038/nature14328 · Cited by 611

The ubiquitin ligase parkin mediates resistance to intracellular pathogens

Manzanillo, P. S., Ayres, J. S., Watson, R. O., Collins, A. C., Souza, G., Rae, C. S., Schneider, D. S., Nakamura, K., Shiloh, M. U., & Cox, J. S. (2013) · Nature · doi:10.1038/nature12566 · Cited by 588

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

A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins

Polo, S., Sigismund, S., Faretta, M., Guidi, M., Capua, M. R., Bossi, G., Chen, H., De Camilli, P., & Di Fiore, P. P. (2002) · Nature · doi:10.1038/416451a · Cited by 571

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

Ubiquitin-Binding Protein RAP80 Mediates BRCA1-Dependent DNA Damage Response

Kim, H., Chen, J., & Yu, X. (2007) · Science · doi:10.1126/science.1139621 · Cited by 540

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

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 507

Enhanced Protein Degradation by Branched Ubiquitin Chains

Meyer, H., & Rapé, M. (2014) · Cell · doi:10.1016/j.cell.2014.03.037 · Cited by 493

Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Kalb, R., Latwiel, S., Baymaz, H. I., Jansen, P. W. T. C., Müller, C. W., Vermeulen, M., & Müller, J. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2833 · Cited by 492

Role of a ribosome-associated E3 ubiquitin ligase in protein quality control

Bengtson, M. H., & Joazeiro, C. A. P. (2010) · Nature · doi:10.1038/nature09371 · Cited by 483

Mechanism of phospho-ubiquitin-induced PARKIN activation

Wauer, T., Šimíček, M., Schubert, A. F., & Komander, D. (2015) · Nature · doi:10.1038/nature14879 · Cited by 482

Arrestin-Related Ubiquitin-Ligase Adaptors Regulate Endocytosis and Protein Turnover at the Cell Surface

Lin, C. H., MacGurn, J. A., Chu, T., Stefan, C. J., & Emr, S. D. (2008) · Cell · doi:10.1016/j.cell.2008.09.025 · Cited by 466

Molecular basis of USP7 inhibition by selective small-molecule inhibitors.

Turnbull, A. P., Ioannidis, S., Krajewski, W. W., Pinto-Fernandez, A., Heride, C., Martin, A. C. L., Tonkin, L. M., Townsend, E. C., Buker, S. M., Lancia, D. R., et al. (2017) · Nature · doi:10.1038/nature24451 · Cited by 463

The E3 ligase Cbl-b and TAM receptors regulate cancer metastasis via natural killer cells

Paolino, M., Choidas, A., Wallner, S., Pranjic, B., Uribesalgo, I., Loeser, S., Jamieson, A. M., Langdon, W. Y., Ikeda, F., Fededa, J. P., et al. (2014) · Nature · doi:10.1038/nature12998 · Cited by 456

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 441

Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage

Thorslund, T., Ripplinger, A., Hoffmann, S., Wild, T., Uckelmann, M., Villumsen, B. H., Narita, T., Sixma, T. K., Choudhary, C., Bekker‐Jensen, S., et al. (2015) · Nature · doi:10.1038/nature15401 · Cited by 438

Mobilization of Processed, Membrane-Tethered SPT23 Transcription Factor by CDC48UFD1/NPL4, a Ubiquitin-Selective Chaperone

Rapé, M., Hoppe, T., Gorr, I. H., Kalocay, M., Richly, H., & Jentsch, S. (2001) · Cell · doi:10.1016/s0092-8674(01)00595-5 · Cited by 438

Uhrf1-dependent H3K23 ubiquitylation couples maintenance DNA methylation and replication

Nishiyama, A., Yamaguchi, L., Sharif, J., Johmura, Y., Kawamura, T., Nakanishi, K., Shimamura, S., Arita, K., Kodama, T., Ishikawa, F., et al. (2013) · Nature · doi:10.1038/nature12488 · Cited by 423

Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase

Cadwell, K., & Coscoy, L. (2005) · Science · doi:10.1126/science.1110340 · Cited by 420

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 405

Fbxl10/Kdm2b Recruits Polycomb Repressive Complex 1 to CpG Islands and Regulates H2A Ubiquitylation

Wu, X., Johansen, J. V., & Helin, K. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.016 · Cited by 395

The Core of the Polycomb Repressive Complex Is Compositionally and Functionally Conserved in Flies and Humans

Levine, S. S., Weiss, A., Erdjument‐Bromage, H., Shao, Z., Tempst, P., & Kingston, R. E. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6070-6078.2002 · Cited by 388

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

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

Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1

Nakada, S., Tai, I., Panier, S., Al-Hakim, A., Iemura, S.-I., Juang, Y.-C., O’Donnell, L., Kumakubo, A., Munro, M., Sicheri, F., et al. (2010) · Nature · doi:10.1038/nature09297 · Cited by 357

Coordinated regulation of protein synthesis and degradation by mTORC1

Zhang, Y., Nicholatos, J., Dreier, J. R., Ricoult, S. J. H., Widenmaier, S. B., Hotamisligil, G. S., Kwiatkowski, D. J., & Manning, B. D. (2014) · Nature · doi:10.1038/nature13492 · Cited by 350

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

Targeting Polycomb to Pericentric Heterochromatin in Embryonic Stem Cells Reveals a Role for H2AK119u1 in PRC2 Recruitment

Cooper, S., Dienstbier, M., Hassan, R., Schermelleh, L., Sharif, J., Blackledge, N. P., Marco, V. D., Elderkin, S., Koseki, H., Klose, R. J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.012 · Cited by 349

The deubiquitinase OTULIN is an essential negative regulator of inflammation and autoimmunity

Damgaard, R. B., Walker, J. A., Marco-Casanova, P., Morgan, N. V., Titheradge, H. L., Elliott, P. R., McHale, D., Maher, E. R., McKenzie, A. N. J., & Komander, D. (2016) · Cell · doi:10.1016/j.cell.2016.07.019 · Cited by 348

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 347

von Hippel-Lindau Disease

Kaelin, W. G. (2006) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.2.010506.092049 · Cited by 346

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 344

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

USP7 small-molecule inhibitors interfere with ubiquitin binding.

Kategaya, L., Di Lello, P., Rougé, L., Pastor, R., Clark, K. R., Drummond, J., Kleinheinz, T., Lin, E., Upton, J.-P., Prakash, S., et al. (2017) · Nature · doi:10.1038/nature24006 · Cited by 333

Ubiquitin-dependent regulation of COPII coat size and function

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Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control

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