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 · see citing works

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 · see citing works

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 · 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

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

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 · see citing works

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 1,770 · 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

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 1,512 · 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

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

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 · see citing works

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 1,153 · see citing works

The increasing complexity of the ubiquitin code

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

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 1,035 · see citing works

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 1,027 · 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

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 · 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

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 · see citing works

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 · see citing works

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 938 · see citing works

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 900 · 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

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 · see citing works

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 · see citing works

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 · see citing works

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 847 · see citing works

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 · see citing works

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 · 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

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 805 · see citing works

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 · 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

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

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 734 · see citing works

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 · see citing works

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 · see citing works

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 693 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 668 · see citing works

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 653 · see citing works

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., Camilli, P. V. D., & Fiore, P. P. D. (2002) · Nature · doi:10.1038/416451a · Cited by 633 · see citing works

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 631 · see citing works

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 608 · see citing works

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 594 · see citing works

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 · 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

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

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 · 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

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

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

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 470 · 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

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 · see citing works

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 · see citing works

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 · see citing works

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 451 · see citing works

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 · 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

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 413 · see citing works

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 410 · see citing works

Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase

Cadwell, K., & Coscoy, L. (2005) · Science · doi:10.1126/science.1110340 · Cited by 406 · 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

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 · see citing works

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 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

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

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 · 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

Coordinated regulation of protein synthesis and degradation by mTORC1

Zhang, Y., Nicholatos, J. W., Dreier, J. R., Ricoult, S. J. H., Widenmaier, S. B., Hotamışlıgil, G. S., Kwiatkowski, D. J., & Manning, B. D. (2014) · Nature · doi:10.1038/nature13492 · Cited by 349 · see citing works

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 · 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

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 335 · 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

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 · 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

Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome

McGinty, R. K., Henrici, R. C., & Tan, S. (2014) · Nature · doi:10.1038/nature13890 · Cited by 324 · see citing works

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 323 · see citing works

The Human Homolog of Yeast BRE1 Functions as a Transcriptional Coactivator through Direct Activator Interactions

Kim, J., Hake, S. B., & Roeder, R. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.11.012 · Cited by 317 · see citing works

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

Yau, R. G., Dörner, K., Castellanos, E. R., Haakonsen, D. L., Werner, A. A., Wang, N., Yang, X. W., Martinez-Martín, N., Matsumoto, M. L., Dixit, V. M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.040 · Cited by 315 · see citing works

Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex

Bodnar, N. O., & Rapoport, T. A. (2017) · Cell · doi:10.1016/j.cell.2017.04.020 · Cited by 312 · see citing works

Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy

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

UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome

Hjerpe, R., Bett, J. S., Keuss, M. J., Solovyova, A. S., McWilliams, T. G., Johnson, C., Sahu, I., Varghese, J., Wood, N. T., Wightman, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.001 · Cited by 310 · see citing works

MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5′ end resection

Boersma, V., Moatti, N., Segura‐Bayona, S., Peuscher, M. H., van der Torre, J., Wevers, B. A., Orthwein, A., Durocher, D., & Jacobs, J. J. L. (2015) · Nature · doi:10.1038/nature14216 · 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

Rqc2p and 60 S ribosomal subunits mediate mRNA-independent elongation of nascent chains

Shen, P. S., Park, J. H., Qin, Y., Li, X., Parsawar, K., Larson, M. H., Cox, J. E., Cheng, Y., Lambowitz, A. M., Weissman, J. S., et al. (2015) · Science · doi:10.1126/science.1259724 · Cited by 295 · see citing works

K63 ubiquitylation triggers proteasomal degradation by seeding branched ubiquitin chains

Ohtake, F., Tsuchiya, H., Saeki, Y., & Tanaka, K. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716673115 · Cited by 294 · see citing works

Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination

Bhogaraju, S., Kalayil, S., Liu, Y., Bonn, F., Colby, T., Matić, I., & Đikić, I. (2016) · Cell · doi:10.1016/j.cell.2016.11.019 · Cited by 293 · see citing works

Similarity of sli-1 , a Regulator of Vulval Development in C. elegans , to the Mammalian Proto-Oncogene c- cbl

Yoon, C. H., Lee, J., Jongeward, G. D., & Sternberg, P. W. (1995) · Science · doi:10.1126/science.7652556 · Cited by 291 · see citing works

A novel site for ubiquitination: the N‐terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein

Breitschopf, K., Bengal, E., Ziv, T., Admon, A., & Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.5964 · Cited by 284 · see citing works

PCGF3/5–PRC1 initiates Polycomb recruitment in X chromosome inactivation

Almeida, M. R., Pintacuda, G., Masui, O., Koseki, Y., Gdula, M. R., Cerase, A., Brown, D., Mould, A. W., Innocent, C., Nakayama, M., et al. (2017) · Science · doi:10.1126/science.aal2512 · Cited by 284 · see citing works

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity

Pao, K., Wood, N. T., Knebel, A., Rafie, K., Stanley, M., Mabbitt, P. D., Sundaramoorthy, R., Hofmann, K., van Aalten, D. M. F., & Virdee, S. (2018) · Nature · doi:10.1038/s41586-018-0026-1 · Cited by 282 · 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

Degradation-Mediated Protein Quality Control in the Nucleus

Gardner, R. G., Nelson, Z. W., & Gottschling, D. E. (2005) · Cell · doi:10.1016/j.cell.2005.01.016 · Cited by 280 · see citing works

The Processivity of Multiubiquitination by the APC Determines the Order of Substrate Degradation

Rapé, M., Reddy, S., & Kirschner, M. W. (2006) · Cell · doi:10.1016/j.cell.2005.10.032 · 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

Control of Protein Quality and Stoichiometries by N-Terminal Acetylation and the N-End Rule Pathway

Shemorry, A., Hwang, C., & Varshavsky, A. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.018 · Cited by 276 · see citing works

Protein targeting and degradation are coupled for elimination of mislocalized proteins

Hessa, T., Sharma, A., Mariappan, M., Eshleman, H. D., Gutierrez, E., & Hegde, R. S. (2011) · Nature · doi:10.1038/nature10181 · Cited by 272 · see citing works

Oligomerization of p62 allows for selection of ubiquitinated cargo and isolation membrane during selective autophagy

Wurzer, B., Zaffagnini, G., Fracchiolla, D., Turco, E., Abert, C., Romanov, J., & Martens, S. (2015) · eLife · doi:10.7554/elife.08941 · Cited by 271 · see citing works

A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response

Ashida, H., Kim, M., Schmidt‐Supprian, M., Ma, A. I., Ogawa, M., & Sasakawa, C. (2009) · Nature Cell Biology · doi:10.1038/ncb2006 · Cited by 264 · see citing works

Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1

Heck, J. W., Cheung, S. K., & Hampton, R. Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910591107 · Cited by 259 · see citing works

DNA methylation requires a DNMT1 ubiquitin interacting motif (UIM) and histone ubiquitination

Qin, W., Wolf, P., Liu, N., Link, S., Smets, M., Mastra, F. L., Forné, I., Pichler, G., Hörl, D., Fellinger, K., et al. (2015) · Cell Research · doi:10.1038/cr.2015.72 · Cited by 259 · see citing works

Ubiquilins Chaperone and Triage Mitochondrial Membrane Proteins for Degradation

Itakura, E., Zavodszky, E., Shao, S., Wohlever, M. L., Keenan, R. J., & Hegde, R. S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.020 · Cited by 255 · 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

Direct, Noncatalytic Mechanism of IKK Inhibition by A20

Skaug, B. A., Chen, J., Du, F., He, J., Ma, A. I., & Chen, Z. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.015 · Cited by 246 · 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

PRP19 Transforms into a Sensor of RPA-ssDNA after DNA Damage and Drives ATR Activation via a Ubiquitin-Mediated Circuitry

Maréchal, A., Li, J.-M., Ji, X. Y., Wu, C.-S. P., Yazinski, S. A., Nguyen, H. D., Liu, S., Jiménez, A. E., Jin, J., & Zou, L. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.11.002 · Cited by 246 · 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

A mouse forward genetics screen identifies LISTERIN as an E3 ubiquitin ligase involved in neurodegeneration

Chu, J., Hong, N. A., Masuda, C. A., Jenkins, B., Nelms, K. A., Goodnow, C. C., Glynne, R. J., Wu, H., Masliah, E., Joazeiro, C. A. P., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812819106 · Cited by 238 · see citing works

The structural basis of modified nucleosome recognition by 53BP1

Wilson, M. D., Benlekbir, S., Fradet‐Turcotte, A., Sherker, A., Julien, J., McEwan, A., Noordermeer, S. M., Sicheri, F., Rubinstein, J. L., & Durocher, D. (2016) · Nature · doi:10.1038/nature18951 · Cited by 234 · see citing works

RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear fociPreprint

Hu, Y., Scully, R., Sobhian, B., Xie, A., Shestakova, E. A., & Livingston, D. M. (2011) · Genes & Development · doi:10.1101/gad.2011011 · Cited by 232 · see citing works

Structure and Assembly Pathway of the Ribosome Quality Control Complex

Shao, S., Brown, A., Santhanam, B., & Hegde, R. S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.015 · Cited by 225 · see citing works

Detection of sequential polyubiquitylation on a millisecond timescale

Pierce, N. W., Kleiger, G., Shan, S., & Deshaies, R. J. (2009) · Nature · doi:10.1038/nature08595 · Cited by 225 · see citing works

Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination

Liu, C.-C., Lin, Y., Chen, Y.-H., Chen, C., Pang, L.-Y., Chen, H.-A., Wu, P., Lin, M.-Y., Jiang, S., Tsai, T., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.11.001 · Cited by 224 · see citing works

Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells

Lee, J., Takahama, S., Zhang, G., Tomarev, S. I., & Ye, Y. (2016) · Nature Cell Biology · doi:10.1038/ncb3372 · Cited by 217 · see citing works

RNF20 and USP44 Regulate Stem Cell Differentiation by Modulating H2B Monoubiquitylation

Fuchs, G., Shema, E., Vesterman, R., Kotler, E., Wolchinsky, Z., Wilder, S., Golomb, L., Pribluda, A., Zhang, F., Haj‐Yahya, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.023 · Cited by 214 · see citing works

LUBAC-synthesized linear ubiquitin chains restrict cytosol-invading bacteria by activating autophagy and NF-κB

Noad, J., von der Malsburg, A., Pathe, C., Michel, M. A., Komander, D., & Randow, F. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.63 · Cited by 214 · see citing works

Mechanism and regulation of the Lys6-selective deubiquitinase USP30

Gersch, M., Gladkova, C., Schubert, A. F., Michel, M. A., Maslen, S., & Komander, D. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3475 · Cited by 214 · 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

TORC1 Regulates Endocytosis via Npr1-Mediated Phosphoinhibition of a Ubiquitin Ligase Adaptor

MacGurn, J. A., Hsu, P.-C., Smolka, M. B., & Emr, S. D. (2011) · Cell · doi:10.1016/j.cell.2011.09.054 · Cited by 203 · see citing works

Listerin-Dependent Nascent Protein Ubiquitination Relies on Ribosome Subunit Dissociation

Shao, S., von der Malsburg, K., & Hegde, R. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.015 · Cited by 201 · see citing works

NEMO specifically recognizes K63‐linked poly‐ubiquitin chains through a new bipartite ubiquitin‐binding domain

Laplantine, E., Fontan, E., Chiaravalli, J., Lopez, T. E., Lakisic, G., Véron, M., Agou, F., & Israël, A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.241 · Cited by 201 · see citing works

Transcriptional repression by PRC1 in the absence of H2A monoubiquitylationPreprint

Pengelly, A. R., Kalb, R., Finkl, K., & Müller, J. (2015) · Genes & Development · doi:10.1101/gad.265439.115 · Cited by 200 · see citing works

A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins

Sung, M., Porras-Yakushi, T. R., Reitsma, J. M., Huber, F. M., Sweredoski, M. J., Hoelz, A., Hess, S. Y., & Deshaies, R. J. (2016) · eLife · doi:10.7554/elife.19105 · Cited by 195 · see citing works

Molecular mechanisms of coupled monoubiquitination

Woelk, T., Oldrini, B., Maspero, E., Confalonieri, S., Cavallaro, E. C., Fiore, P. P. D., & Polo, S. (2006) · Nature Cell Biology · doi:10.1038/ncb1484 · Cited by 192 · see citing works

A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication

Kotewicz, K. M., Ramabhadran, V., Sjoblom, N. M., Vogel, J. P., Haenssler, E., Zhang, M., Behringer, J., Scheck, R. A., & Isberg, R. R. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.12.007 · Cited by 192 · see citing works

Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling

Michel, M. A., Swatek, K. N., Hospenthal, M. K., & Komander, D. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.020 · Cited by 192 · see citing works

Structure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance

Ishiyama, S., Nishiyama, A., Saeki, Y., Moritsugu, K., Morimoto, D., Yamaguchi, L., Arai, N., Matsumura, R., Kawakami, T., Mishima, Y., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.037 · Cited by 192 · see citing works

Cysteine methylation disrupts ubiquitin-chain sensing in NF-κB activation

Zhang, L., Ding, X., Cui, J., Xu, H., Chen, J., Gong, Y., Hu, L., Zhou, Y. W., Ge, J., Lu, Q., et al. (2011) · Nature · doi:10.1038/nature10690 · 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

Disorder Targets Misorder in Nuclear Quality Control Degradation: A Disordered Ubiquitin Ligase Directly Recognizes Its Misfolded Substrates

Rosenbaum, J. C., Fredrickson, E. K., Oeser, M. L., Garrett-Engele, C. M., Locke, M. N., Richardson, L. A., Nelson, Z. W., Hetrick, E. D., Milac, T. I., Gottschling, D. E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.004 · Cited by 187 · see citing works

Cytosolic Quality Control of Mislocalized Proteins Requires RNF126 Recruitment to Bag6

Rodrigo-Brenni, M. C., Gutierrez, E., & Hegde, R. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.025 · Cited by 186 · 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

The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response

Sanada, T., Kim, M., Mimuro, H., Suzuki, M., Ogawa, M., Oyama, A., Ashida, H., Kobayashi, T., Koyama, T., Nagai, S., et al. (2012) · Nature · doi:10.1038/nature10894 · Cited by 183 · see citing works

An evolutionarily conserved pathway controls proteasome homeostasis

Rousseau, A., & Bertolotti, A. (2016) · Nature · doi:10.1038/nature18943 · Cited by 182 · see citing works

A Cotranslational Ubiquitination Pathway for Quality Control of Misfolded Proteins

Wang, F., Durfee, L. A., & Huibregtse, J. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.009 · Cited by 179 · see citing works

Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting

Hirano, S., Kawasaki, M., Ura, H., Kato, R., Raiborg, C., Stenmark, H., & Soichi Wakatsuki, A. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1051 · Cited by 178 · see citing works

Structure of PINK1 in complex with its substrate ubiquitin

Schubert, A. F., Gladkova, C., Pardon, E., Wagstaff, J. L., Freund, S. M. V., Steyaert, J., Maslen, S., & Komander, D. (2017) · Nature · doi:10.1038/nature24645 · Cited by 178 · see citing works

Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy

Blythe, E. E., Olson, K. C., Chau, V., & Deshaies, R. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706205114 · Cited by 176 · see citing works

Linear ubiquitination of cytosolic Salmonella Typhimurium activates NF-κB and restricts bacterial proliferation

van Wijk, S. J. L., Fricke, F., Herhaus, L., Gupta, J., Hötte, K., Pampaloni, F., Grumati, P., Kaulich, M., Sou, Y., Komatsu, M., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.66 · Cited by 172 · see citing works

ESCRT-dependent cargo sorting at multivesicular endosomes

Frankel, E. B., & Audhya, A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.08.020 · Cited by 172 · see citing works

BBAP Monoubiquitylates Histone H4 at Lysine 91 and Selectively Modulates the DNA Damage Response

Yan, Q., Dutt, S., Xu, R., Graves, K., Juszczyński, P., Manis, J. P., & Shipp, M. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.019 · Cited by 165 · see citing works

UBE2O remodels the proteome during terminal erythroid differentiation

Nguyen, A. T., Prado, M. A., Schmidt, P. J., Sendamarai, A. K., Wilson‐Grady, J., Min, M., Campagna, D. R., Tian, G., Shi, Y., Dederer, V., et al. (2017) · Science · doi:10.1126/science.aan0218 · Cited by 164 · see citing works

K29-Selective Ubiquitin Binding Domain Reveals Structural Basis of Specificity and Heterotypic Nature of K29 Polyubiquitin

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

CAT-tailing as a fail-safe mechanism for efficient degradation of stalled nascent polypeptides

Kostova, K. K., Hickey, K. L., Osuna, B. A., Hussmann, J. A., Frost, A. S., Weinberg, D. E., & Weissman, J. S. (2017) · Science · doi:10.1126/science.aam7787 · Cited by 160 · see citing works

The N-Terminal Methionine of Cellular Proteins as a Degradation Signal

Kim, H.-K., Kim, R.-R., Oh, J., Cho, H., Varshavsky, A. J., & Hwang, C. (2013) · Cell · doi:10.1016/j.cell.2013.11.031 · Cited by 159 · see citing works

Building a Regulatory Network with Short Linear Sequence Motifs: Lessons from the Degrons of the Anaphase-Promoting Complex

Davey, N. E., & Morgan, D. O. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.006 · Cited by 158 · see citing works

The E3 ubiquitin ligase activity of RING1B is not essential for early mouse developmentPreprint

Illingworth, R. S., Moffat, M., Mann, A. R., Read, D., Hunter, C. J., Pradeepa, M. M., Adams, I. R., & Bickmore, W. A. (2015) · Genes & Development · doi:10.1101/gad.268151.115 · Cited by 157 · see citing works

Genomic Models of Metastatic Cancer: Functional Analysis of Death-from-Cancer Signature Genes Reveals Aneuploid, Anoikis-Resistant, Metastasis-Enabling Phenotype with Altered Cell Cycle Control and Activated PcG Protein Chromatin Silencing Pathway

Glinsky, G. V. (2006) · Cell Cycle · doi:10.4161/cc.5.11.2796 · Cited by 157 · see citing works

Fluorescence-Based Sensors to Monitor Localization and Functions of Linear and K63-Linked Ubiquitin Chains in Cells

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

AMBRA1 Interplay with Cullin E3 Ubiquitin Ligases Regulates Autophagy Dynamics

Antonioli, M., Albiero, F., Nazio, F., Vescovo, T., Perdomo, A. B., Corazzari, M., Marsella, C., Piselli, P., Gretzmeier, C., Dengjel, J., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.11.013 · Cited by 155 · see citing works

SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling

Elliott, P. R., Leske, D., Hrdinka, M., Bagola, K., Fiil, B. K., McLaughlin, S. H., Wagstaff, J. L., Volkmar, N., Christianson, J. C., Kessler, B. M., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.001 · Cited by 155 · see citing works

The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases

Pruneda, J. N., Durkin, C. H., Geurink, P. P., Ovaa, H., Santhanam, B., Holden, D. W., & Komander, D. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.015 · Cited by 154 · see citing works

Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.

Panier, S., Ichijima, Y., Fradet-Turcotte, A., Leung, C. C. Y., Kaustov, L., Arrowsmith, C. H., & Durocher, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.045 · Cited by 152 · see citing works

ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth

Atanassov, B. S., Mohan, R. D., Lan, X., Kuang, X., Lu, Y., Lin, K., McIvor, E., Li, W., Zhang, Y., Florens, L. A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.030 · Cited by 151 · see citing works

The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins

Higgins, R., Gendron, J. M., Rising, L., Mak, R., Webb, K. J., Kaiser, S. E., Zuzow, N., Riviere, P. J., Yang, B., Fenech, E. J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.026 · Cited by 149 · see citing works

The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases

Hwang, C., Shemorry, A., Auerbach, D., & Varshavsky, A. J. (2010) · Nature Cell Biology · doi:10.1038/ncb2121 · Cited by 147 · see citing works

Mechanism of APC/C CDC20 activation by mitotic phosphorylation

Qiao, R., Weissmann, F., Yamaguchi, M., Brown, N. G., VanderLinden, R. T., Imre, R., Jarvis, M. A., Brunner, M. R., Davidson, I. F., Litos, G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604929113 · Cited by 143 · see citing works

The RNF138 E3 ligase displaces Ku to promote DNA end resection and regulate DNA repair pathway choice

Ismail, I. H., Gagné, J., Genois, M., Strickfaden, H., McDonald, D., Xu, Z., Poirier, G. G., Masson, J., & Hendzel, M. J. (2015) · Nature Cell Biology · doi:10.1038/ncb3259 · Cited by 142 · see citing works

Ubiquitylation of an ERAD Substrate Occurs on Multiple Types of Amino Acids

Shimizu, Y., Okuda-Shimizu, Y., & Hendershot, L. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.033 · Cited by 139 · see citing works

Usp16 contributes to somatic stem-cell defects in Down’s syndrome

Adorno, M., Sikandar, S. S., Mitra, S. S., Kuo, A. H., di Robilant, B. N., Acosta, V. H., Ouadah, Y., Quarta, M., Rodriguez, J., Qian, D., et al. (2013) · Nature · doi:10.1038/nature12530 · 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

Mechanistic basis for a molecular triage reaction

Shao, S., Rodrigo-Brenni, M. C., Kivlen, M. H., & Hegde, R. S. (2017) · Science · doi:10.1126/science.aah6130 · Cited by 135 · see citing works

The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover

Tawo, R., Pokrzywa, W., Kevei, É., Akyuz, M. E., Balaji, V., Adrian, S., Höhfeld, J., & Hoppe, T. (2017) · Cell · doi:10.1016/j.cell.2017.04.003 · Cited by 134 · see citing works

UBE2O is a quality control factor for orphans of multiprotein complexes

Yanagitani, K., Juszkiewicz, S., & Hegde, R. S. (2017) · Science · doi:10.1126/science.aan0178 · Cited by 132 · see citing works

Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex

Lyumkis, D., Passos, D. O., Tahara, E. B., Webb, K. J., Bennett, E. J., Vinterbo, S. A., Potter, C. S., Carragher, B. O., & Joazeiro, C. A. P. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413882111 · Cited by 130 · see citing works

RFWD3-Dependent Ubiquitination of RPA Regulates Repair at Stalled Replication Forks

Elia, A. E. H., Wang, D. C., Willis, N. A., Boardman, A. P., Hajdú, I., Adeyemi, R. O., Lowry, E. L., Gygi, S. P., Scully, R., & Elledge, S. J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.011 · Cited by 129 · see citing works

Regulation of the CUL3 Ubiquitin Ligase by a Calcium-Dependent Co-adaptor

McGourty, C. A., Akopian, D., Walsh, C., Gorur, A., Werner, A., Schekman, R., Bautista, D., & Rape, M. (2016) · Cell · doi:10.1016/j.cell.2016.09.026 · Cited by 126 · see citing works

STAM Proteins Bind Ubiquitinated Proteins on the Early Endosome via the VHS Domain and Ubiquitin-interacting Motif

Mizuno, E., Kawahata, K., Kato, M., Kitamura, N., & Komada, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0823 · Cited by 125 · see citing works

Protein Quality Control of the Endoplasmic Reticulum and Ubiquitin–Proteasome-Triggered Degradation of Aberrant Proteins: Yeast Pioneers the Path

Berner, N., Reutter, K., & Wolf, D. H. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012749 · Cited by 125 · see citing works

Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains

Liu, C., Liu, W., Ye, Y., & Li, W. (2017) · Nature Communications · doi:10.1038/ncomms14274 · Cited by 122 · see citing works

Systematic E2 screening reveals a UBE2D–RNF138–CtIP axis promoting DNA repair

Schmidt, C. K., Galanty, Y., Sczaniecka-Clift, M., Coates, J., Jhujh, S. S., Demir, M., Cornwell, M., Beli, P., & Jackson, S. P. (2015) · Nature Cell Biology · doi:10.1038/ncb3260 · Cited by 119 · see citing works

The Met1-Linked Ubiquitin Machinery: Emerging Themes of (De)regulation

Hrdinka, M., & Gyrd‐Hansen, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.001 · Cited by 118 · see citing works

Global Analysis of Host and Bacterial Ubiquitinome in Response to Salmonella Typhimurium Infection

Fiskin, E., Bionda, T., Dikic, I., & Behrends, C. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.015 · Cited by 114 · see citing works

ESCRTs function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteins

Zhu, L., Jorgensen, J. R., Li, M., Chuang, Y.-S., & Emr, S. D. (2017) · eLife · doi:10.7554/elife.26403 · Cited by 112 · 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

Shigella flexneri suppresses NF-κB activation by inhibiting linear ubiquitin chain ligation

de Jong, M. F., Liu, Z., Chen, D., & Alto, N. M. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.84 · Cited by 105 · see citing works

USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A

Uckelmann, M., Densham, R. M., Baas, R., Winterwerp, H. H. K., Fish, A., Sixma, T. K., & Morris, J. R. (2018) · Nature Communications · doi:10.1038/s41467-017-02653-3 · Cited by 101 · see citing works

COPII-coated membranes function as transport carriers of intracellular procollagen I

Gorur, A., Yuan, L., Kenny, S. J., Baba, S., Xu, K., & Schekman, R. W. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201702135 · Cited by 99 · see citing works

Lys63/Met1-hybrid ubiquitin chains are commonly formed during the activation of innate immune signalling

Emmerich, C. H., Bakshi, S., Kelsall, I. R., Ortiz-Guerrero, J., Shpiro, N., & Cohen, P. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.141 · Cited by 97 · see citing works

Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p

Williams, C., van den Berg, M., Geers, E., & Distel, B. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.054 · Cited by 90 · see citing works

Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair

Zhao, Y. J., Brickner, J. R., Majid, M. C., & Mosammaparast, N. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.01.005 · Cited by 78 · see citing works

Targeted large‐scale analysis of protein acetylation

Mischerikow, N., & Heck, A. J. R. (2010) · PROTEOMICS · doi:10.1002/pmic.201000397 · Cited by 78 · see citing works

USP9X Controls EGFR Fate by Deubiquitinating the Endocytic Adaptor Eps15

Savio, M. G., Wollscheid, N., Cavallaro, E. C., Algisi, V., Fiore, P. P. D., Sigismund, S., Maspero, E., & Polo, S. (2015) · Current Biology · doi:10.1016/j.cub.2015.11.050 · Cited by 76 · see citing works

CRL2 aids elimination of truncated selenoproteins produced by failed UGA/Sec decoding

Lin, H.-C., Ho, S.-C., Chen, Y.-Y., Khoo, K., Hsu, P., & Yen, H.-C. S. (2015) · Science · doi:10.1126/science.aab0515 · Cited by 75 · see citing works

Deubiquitinases Sharpen Substrate Discrimination during Membrane Protein Degradation from the ER

Zhang, Z.-R., Bonifacino, J. S., & Hegde, R. S. (2013) · Cell · doi:10.1016/j.cell.2013.06.038 · Cited by 71 · see citing works

Ubiquitination of Substrates by Esterification

Wang, X., Herr, R. A., & Hansen, T. H. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01269.x · Cited by 70 · see citing works

PROTAC targeted protein degraders: the past is prologue

Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works

The BioGRID interaction database: 2019 update

Oughtred, R., Stark, C., Breitkreutz, B., Rust, J., Boucher, L., Chang, C., Kolas, N. K., O’Donnell, L., Leung, G. C., McAdam, R. F., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1079 · Cited by 1,440 · see citing works

Cellular quality control by the ubiquitin-proteasome system and autophagy

Pohl, C., & Đikić, I. (2019) · Science · doi:10.1126/science.aax3769 · Cited by 1,229 · see citing works

Advancing targeted protein degradation for cancer therapy

Dale, B., Cheng, M., Park, K., Kanıskan, H. Ü., Xiong, Y., & Jin, J. J. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00365-x · Cited by 671 · see citing works

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449 · 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

An expanded lexicon for the ubiquitin code

Đikić, I., & Schulman, B. A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00543-1 · Cited by 417 · see citing works

Protein quality control in the secretory pathway

Sun, Z., & Brodsky, J. L. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201906047 · Cited by 381 · see citing works

Beyond K48 and K63: non-canonical protein ubiquitination

Tracz, M., & Białek, W. (2021) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00245-6 · Cited by 352 · see citing works

Histone Ubiquitination: An Integrative Signaling Platform in Genome Stability

Mattiroli, F., & Penengo, L. (2021) · Trends in Genetics · doi:10.1016/j.tig.2020.12.005 · Cited by 240 · see citing works

Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation

Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 230 · see citing works

The Ubiquitin–Proteasome System in Immune Cells

Çetin, G., Klafack, S., Studencka‐Turski, M., Krüger, E., & Ebstein, F. (2021) · Biomolecules · doi:10.3390/biom11010060 · Cited by 210 · see citing works

A Cellular Mechanism to Detect and Alleviate Reductive Stress.

Manford, A., Rodríguez-Pérez, F., Shih, K. Y., Shi, Z., Berdan, C. A., Choe, M., Titov, D., Nomura, D., & Rapé, M. (2020) · Cell · doi:10.1016/j.cell.2020.08.034 · Cited by 185 · see citing works

Emerging functions of branched ubiquitin chains

French, M., Koehler, C. F., & Hunter, T. R. (2021) · Cell Discovery · doi:10.1038/s41421-020-00237-y · Cited by 194 · see citing works

Extracellular targeted protein degradation: an emerging modality for drug discovery

Wells, J. A., & Kumru, K. S. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00833-z · Cited by 190 · see citing works

Expanding the arsenal of E3 ubiquitin ligases for proximity-induced protein degradation

Kannt, A., & Đikić, I. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.007 · Cited by 149 · see citing works

A conserved SUMO pathway repairs topoisomerase DNA-protein cross-links by engaging ubiquitin-mediated proteasomal degradation

Sun, Y., Jenkins, L. M. M., Su, Y. P., Nitiss, K. C., Nitiss, J. L., & Pommier, Y. G. (2020) · Science Advances · doi:10.1126/sciadv.aba6290 · Cited by 150 · see citing works

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation

Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 144 · see citing works

Time-resolved in vivo ubiquitinome profiling by DIA-MS reveals USP7 targets on a proteome-wide scale

Steger, M., Demichev, V., Backman, M., Ohmayer, U., Ihmor, P., Müller, S., Ralser, M., & Daub, H. (2021) · Nature Communications · doi:10.1038/s41467-021-25454-1 · Cited by 147 · see citing works

HECT E3 Ligases: A Tale With Multiple Facets

Weber, J., Polo, S., & Maspero, E. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00370 · Cited by 143 · see citing works

The Roles of Ubiquitin in Mediating Autophagy

Yin, Z., Popelka, H., Lei, Y., Yang, Y., & Klionsky, D. J. (2020) · Cells · doi:10.3390/cells9092025 · Cited by 133 · see citing works

Targeting the signaling in Epstein–Barr virus-associated diseases: mechanism, regulation, and clinical study

Cao, Y., Xie, L.-L., Shi, F., Tang, M., Li, Y.-S., Hu, J., Zhao, L., Zhao, L.-Q., Yu, X., Luo, X.-J., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00376-4 · Cited by 115 · see citing works

Oxidation and alkylation stresses activate ribosome-quality control

Yan, L. L., Simms, C. L., McLoughlin, F., Vierstra, R. D., & Zaher, H. S. (2019) · Nature Communications · doi:10.1038/s41467-019-13579-3 · Cited by 123 · see citing works

TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains

Kaiho-Soma, A., Akizuki, Y., Igarashi, K., Endo, A., Shoda, T., Kawase, Y., Demizu, Y., Naito, M., Saeki, Y., Tanaka, K., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.023 · Cited by 110 · see citing works

Assembly and function of branched ubiquitin chains

Kolla, S., Ye, M., Mark, K. G., & Rapé, M. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.04.003 · Cited by 109 · see citing works

Enzymatic Logic of Ubiquitin Chain Assembly

Deol, K. K., Lorenz, S., & Strieter, E. R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00835 · Cited by 107 · see citing works

Structure, Dynamics and Function of the 26S Proteasome

Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 105 · see citing works

UBE2O targets Mxi1 for ubiquitination and degradation to promote lung cancer progression and radioresistance

Huang, Y., Yang, X., Lu, Y., Zhao, Y., Meng, R., Zhang, S., Dong, X., Xu, S., & Wu, G. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00616-8 · Cited by 102 · see citing works

Proteasome in action: substrate degradation by the 26S proteasome

Sahu, I., & Glickman, M. H. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200382 · Cited by 101 · see citing works

Excision repair of topoisomerase DNA-protein crosslinks (TOP-DPC)

Sun, Y., Saha, S. T., Wang, W., Saha, L. K., Huang, S.-Y. N., & Pommier, Y. G. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102837 · Cited by 98 · see citing works

Host-mediated ubiquitination of a mycobacterial protein suppresses immunity

Wang, L., Wu, J., Li, J., Yang, H., Tang, T., Liang, H., Zuo, M., Wang, J., Liu, H., Liu, F., et al. (2020) · Nature · doi:10.1038/s41586-019-1915-7 · Cited by 96 · see citing works

Proteasome-Bound UCH37/UCHL5 Debranches Ubiquitin Chains to Promote Degradation

Deol, K. K., Crowe, S. O., Du, J., Bisbee, H. A., Guenette, R. G., & Strieter, E. R. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.017 · Cited by 89 · see citing works

Stimuli-activatable PROTACs for precise protein degradation and cancer therapy

Gao, J., Yang, L., Lei, S., Zhou, F., Nie, H., Peng, B., Xu, T., Chen, X., Yang, X., Sheng, C., et al. (2023) · 中国科学通报：英文版 · doi:10.1016/j.scib.2023.04.028 · Cited by 87 · see citing works

Chemical Synthesis of Activity‐Based E2‐Ubiquitin Probes for the Structural Analysis of E3 Ligase‐Catalyzed Transthiolation

Liang, L., Chu, G., Qu, Q., Zuo, C., Mao, J., Zheng, Q., Chen, J., Meng, X., Jing, Y., Deng, H., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202105870 · Cited by 85 · see citing works

USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7

Sapmaz, A., Berlin, I., Bos, E., Wijdeven, R. H. M., Janssen, H., Konietzny, R., Akkermans, J. J. L. L., Erson-Bensan, A. E., Koning, R. I., Kessler, B. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09437-x · Cited by 84 · see citing works

Deubiquitinating enzyme amino acid profiling reveals a class of ubiquitin esterases

Cesare, V. D., Carbajo, D., Mabbitt, P. D., Fletcher, A. J., Soetens, M., Antico, O., Wood, N. T., & Virdee, S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006947118 · Cited by 85 · see citing works

Targeting the Ubiquitin–Proteasome System and Recent Advances in Cancer Therapy

Spano, D., & Catara, G. (2023) · Cells · doi:10.3390/cells13010029 · Cited by 85 · see citing works

A20: A multifunctional tool for regulating immunity and preventing disease

Malynn, B. A., & Ma, A. I. (2019) · Cellular Immunology · doi:10.1016/j.cellimm.2019.04.002 · Cited by 80 · see citing works

Membrane Protein Quality Control Mechanisms in the Endo-Lysosome System

Sardana, R., & Emr, S. D. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.11.011 · Cited by 84 · see citing works

A new dawn beyond lysine ubiquitination

Squair, D. R., & Virdee, S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01088-2 · Cited by 81 · see citing works

Comprehensive overview of Nrf2-related epigenetic regulations involved in ischemia-reperfusion injury

Zhang, J., Pan, W., Zhang, Y., Tan, M., Yin, Y., Li, Y., Zhang, L., Han, L., Bai, J., Jiang, T., et al. (2022) · Theranostics · doi:10.7150/thno.77243 · Cited by 81 · see citing works

Structural basis for RING-Cys-Relay E3 ligase activity and its role in axon integrity

Mabbitt, P. D., Loreto, A., Déry, M.-A. C., Fletcher, A. J., Stanley, M., Pao, K., Wood, N. T., Coleman, M. P., & Virdee, S. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0598-6 · Cited by 78 · see citing works

Cellular Protein Aggregates: Formation, Biological Effects, and Ways of Elimination

Wen, J.-H., He, X., Feng, Z.-S., Li, D.-Y., Tang, J., & Liu, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108593 · Cited by 81 · see citing works

Oligomerization‐driven MLKL ubiquitylation antagonizes necroptosis

Liu, Z., Dagley, L. F., Shield‐Artin, K., Young, S. N., Bankovacki, A., Wang, X. S., Tang, M., Howitt, J. A., Stafford, C. A., Nachbur, U., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2019103718 · Cited by 76 · see citing works

Speaking the host language: how Salmonella effector proteins manipulate the host

Pillay, T. D., Hettiarachchi, S. U., Gan, J., Diaz-del-Olmo, I., Yu, X., Muench, J. H., Thurston, T. L. M., & Pearson, J. S. (2023) · Microbiology · doi:10.1099/mic.0.001342 · Cited by 70 · see citing works

Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains

Lu, L., Zhai, X., Li, X., Wang, S., Zhang, L., Wang, L., Jin, X., Liang, L., Deng, Z., Li, Z., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32364-3 · Cited by 72 · see citing works

Recent progress in degradation of membrane proteins by PROTACs and alternative targeted protein degradation techniques

Chen, S., Cui, J., Chen, H., Yu, B., & Long, S. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115911 · Cited by 70 · see citing works

Conservation and similarity of bacterial and eukaryotic innate immunity

Ledvina, H. E., & Whiteley, A. T. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-024-01017-1 · Cited by 70 · see citing works

Development and application of ubiquitin-based chemical probes

Sui, X., Wang, Y., Du, Y., Liang, L., Zheng, Q., Li, Y., & Liu, L. (2020) · Chemical Science · doi:10.1039/d0sc03295f · Cited by 70 · see citing works

An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes

Barbour, H., Nkwe, N. S., Estavoyer, B., Messmer, C., Gushul-Leclaire, M., Villot, R., Uriarte, M., Boulay, K., Hlayhel, S., Farhat, B., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106276 · Cited by 69 · see citing works

Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies

Niemeyer, M., Castillo, E. M., Ihling, C. H., Iacobucci, C., Wilde, V., Hellmuth, A., Hoehenwarter, W., Samodelov, S. L., Zurbriggen, M. D., Kastritis, P. L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16147-2 · Cited by 64 · see citing works

E3 ubiquitin ligase SYVN1 is a key positive regulator for GSDMD-mediated pyroptosis

Shi, Y., Yang, Y., Xu, W., Shi, D., Xu, W., Fu, X., Lv, Q., Xia, J. L., & Shi, F. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04553-x · Cited by 63 · see citing works

Mechanisms of noncanonical binding dynamics in multivalent protein–protein interactions

Errington, W. J., Bruncsics, B., & Sarkar, C. A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902909116 · Cited by 63 · see citing works

Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies

Chen, X., Htet, Z. M., López-Alfonzo, E. M., Martin, A., & Walters, K. J. (2020) · FEBS Journal · doi:10.1111/febs.15638 · Cited by 61 · see citing works

Vasculitis associated with VEXAS syndrome: A literature review

Watanabe, R., Kiji, M., & Hashimoto, M. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.983939 · Cited by 60 · see citing works

Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase

Kong, K.-Y. E., Fischer, B. M., Meurer, M., Kats, I., Li, Z., Rühle, F., Barry, J. D., Kirrmaier, D., Chevyreva, V., Luis, B.-J. S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.018 · Cited by 53 · see citing works

Opportunities for Therapeutic Modulation of O-GlcNAc

Cheng, S. S., Mody, A. C., & Woo, C. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00417 · Cited by 61 · see citing works

Regulation of the endosomal SNX27-retromer by OTULIN

Stangl, A., Elliott, P. R., Pinto-Fernández, A., Bonham, S., Harrison, L., Schaub, A., Kutzner, K., Keusekotten, K., Pfluger, P. T., Oualid, F. E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12309-z · Cited by 56 · see citing works

UBE2J1 inhibits colorectal cancer progression by promoting ubiquitination and degradation of RPS3

Wang, T., Jin, C., Yang, P., Chen, Z., Ji, J., Sun, Q., Yang, S., Feng, Y., Tang, J., & Sun, Y. (2022) · Oncogene · doi:10.1038/s41388-022-02581-7 · Cited by 55 · see citing works

The deubiquitinase USP15 modulates cellular redox and is a therapeutic target in acute myeloid leukemia

Niederkorn, M., Ishikawa, C., Hueneman, K. M., Bartram, J., Stepanchick, E., Bennett, J., Culver-Cochran, A. E., Bolanos, L., Uible, E., Choi, K., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01394-z · Cited by 35 · see citing works

Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1

Luo, Y., Takagi, J., Claus, L. A. N., Zhang, C., Yasuda, S., Hasegawa, Y., Yamaguchi, J., Shan, L., Russinova, E., & Sato, T. (2022) · EMBO Reports · doi:10.15252/embr.202153354 · Cited by 50 · see citing works

Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective

Greene, E. R., Dong, K. C., & Martin, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.004 · Cited by 49 · see citing works

An E1‐Catalyzed Chemoenzymatic Strategy to Isopeptide‐N‐Ethylated Deubiquitylase‐Resistant Ubiquitin Probes

Zheng, Q., Wang, T., Chu, G., Zuo, C., Zhao, R. J., Sui, X., Ye, L., Yu, Y., Chen, J., Wu, X., et al. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202002974 · Cited by 49 · see citing works

USP15 suppresses tumor immunity via deubiquitylation and inactivation of TET2

Chen, L., Smith, M. D., Lv, L., Nakagawa, T., Li, Z., Sun, S., Brown, N. G., Xiong, Y., & Xu, Y. (2020) · Science Advances · doi:10.1126/sciadv.abc9730 · Cited by 48 · see citing works

Deubiquitylases in developmental ubiquitin signaling and congenital diseases

Basar, M. A., Beck, D. B., & Werner, A. A. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00697-5 · Cited by 44 · see citing works

Ubiquitin-dependent remodeling of the actin cytoskeleton drives cell fusion

Rodríguez-Pérez, F., Manford, A. G., Pogson, A. N., Ingersoll, A. J., Martínez-González, B., & Rapé, M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.01.016 · Cited by 46 · see citing works

Shared and distinct mechanisms of UBA1 inactivation across different diseases

Collins, J. C., Magaziner, S. J., English, M., Hassan, B. A., Chen, X., Balanda, N. J., Anderson, M., Lam, A., Fernandez‐Pol, S., Kwong, B. Y., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00046-z · Cited by 45 · 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

How Influenza Virus Uses Host Cell Pathways during Uncoating

Moreira, É. A., Yamauchi, Y., & Matthias, P. (2021) · Cells · doi:10.3390/cells10071722 · Cited by 44 · see citing works

Sugar-mediated non-canonical ubiquitination impairs Nrf1/NFE2L1 activation

Yoshida, Y., Takahashi, T., Ishii, N., Matsuo, I., Takahashi, S., Inoue, H., Endo, A., Tsuchiya, H., Okada, M., Ando, C., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.07.013 · Cited by 42 · see citing works

Linkage-specific deubiquitylation by OTUD5 defines an embryonic pathway intolerant to genomic variation

Beck, D. B., Basar, M. A., Asmar, A. J., Thompson, J. J., Oda, H., Uehara, D. T., Saida, K., Pajusalu, S., Talvik, I., D’Souza, P., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe2116 · Cited by 40 · see citing works

The Conceivable Functions of Protein Ubiquitination and Deubiquitination in Reproduction

Wang, J., Zhou, Q., Ding, J., Yin, T., Ye, P., & Zhang, Y. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.886261 · Cited by 40 · see citing works

USP28 controls SREBP2 and the mevalonate pathway to drive tumour growth in squamous cancer

Maier, C. R., Hartmann, O., Prieto‐Garcia, C., Al-Shami, K. M., Schlicker, L., Vogel, F. C. E., Haid, S., Klann, K., Buck, V., Münch, C., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01173-6 · Cited by 40 · see citing works

New Insights into Oxidative and Reductive Stress Responses and Their Relation to the Anticancer Activity of Selenium-Containing Compounds as Hydrogen Selenide Donors

Krakowiak, A., & Pietrasik, S. (2023) · Biology · doi:10.3390/biology12060875 · Cited by 40 · see citing works

NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62

Furthmann, N., Bader, V., Angersbach, L., Blusch, A., Goel, S., Sánchez‐Vicente, A., Krause, L. J., Chaban, S. A., Grover, P., Trinkaus, V. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-44033-0 · Cited by 39 · see citing works

Adenovirus-mediated ubiquitination alters protein–RNA binding and aids viral RNA processing

Herrmann, C., Dybas, J. M., Liddle, J. C., Price, A. M., Hayer, K. E., Lauman, R., Purman, C. E., Charman, M., Kim, E. T., Garcia, B. A., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0750-9 · Cited by 39 · see citing works

PROTACs, molecular glues and bifunctionals from bench to bedside: Unlocking the clinical potential of catalytic drugs

Maneiro, M., Vita, E. D., Conole, D., Kounde, C. S., Zhang, Q., & Tate, E. W. (2021) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2021.01.002 · Cited by 38 · see citing works

Loss of FBXO31-mediated degradation of DUSP6 dysregulates ERK and PI3K-AKT signaling and promotes prostate tumorigenesis

Duan, S., Moro, L., Qu, R., Simoneschi, D., Cho, H., Jiang, S., Zhao, H., Chang, Q., de Stanchina, E., Arbini, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109870 · Cited by 39 · see citing works

Applications of protein ubiquitylation and deubiquitylation in drug discovery

Chen, Y., Xue, H., & Jin, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107264 · Cited by 38 · see citing works

USP18 Antagonizes Pyroptosis by Facilitating Selective Autophagic Degradation of Gasdermin D

Wang, L., Li, M., Lian, G., Yang, S., Wu, Y., & Cui, J. (2024) · Research · doi:10.34133/research.0380 · Cited by 35 · see citing works

Unanchored Ubiquitin Chains, Revisited

Blount, J. R., Johnson, S. L., & Todi, S. V. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.582361 · Cited by 32 · see citing works

Protein quality control by the proteasome and autophagy: A regulatory role of ubiquitin and liquid-liquid phase separation

Lei, L., Wu, Z., & Winklhofer, K. F. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.11.003 · Cited by 34 · see citing works

The Role of Ubiquitin in Regulating Stress Granule Dynamics

Krause, L. J., Herrera, M. G., & Winklhofer, K. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.910759 · Cited by 30 · see citing works

The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis

Hasegawa, Y., Reyes, T. H., Uemura, T., Baral, A., Fujimaki, A., Luo, Y., Morita, Y., Saeki, Y., Maekawa, S., Yasuda, S., et al. (2022) · The Plant Cell · doi:10.1093/plcell/koac014 · Cited by 33 · see citing works

Mitochondrial control of cellular protein homeostasis

Mohanraj, K., Nowicka, U., & Chacińska, A. (2020) · Biochemical Journal · doi:10.1042/bcj20190654 · Cited by 27 · see citing works

Ubiquitin-specific protease 2a promotes hepatocellular carcinoma progression via deubiquitination and stabilization of RAB1A

Xiong, B., Huang, J., Liu, Y., Zou, M., Zhao, Z., Gong, J., Wu, X., & Qiu, C. (2020) · Cellular Oncology · doi:10.1007/s13402-020-00568-8 · Cited by 32 · see citing works

Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification

Yuan, L., Lv, Z., Adams, M. J., & Olsen, S. K. (2021) · Nature Communications · doi:10.1038/s41467-021-22598-y · Cited by 32 · see citing works

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C

Paluda, A., Middleton, A. J., Roßig, C., Mace, P. D., & Day, C. L. (2022) · Nature Communications · doi:10.1038/s41467-022-28782-y · Cited by 32 · see citing works

USP32-regulated LAMTOR1 ubiquitination impacts mTORC1 activation and autophagy induction.

Hertel, A., Alves, L., Dutz, H., Tascher, G., Bonn, F., Kaulich, M., Dikič, I., Eimer, S., Steinberg, F., & Bremm, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111653 · Cited by 28 · see citing works

Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site

Watson, E. R., Grace, C. R., Zhang, W., Miller, D. J., Davidson, I. F., Prabu, J. R., Yu, S., Bolhuis, D. L., Kulko, E. T., Vollrath, R., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902889116 · Cited by 30 · see citing works

Dynamic Changes to the Skeletal Muscle Proteome and Ubiquitinome Induced by the E3 Ligase, ASB2β

Goodman, C. A., Davey, J. R., Hagg, A., Parker, B. L., & Gregorevic, P. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100050 · Cited by 29 · see citing works

Ubiquitinomics: History, methods, and applications in basic research and drug discovery

Steger, M., Karayel, Ö., & Demichev, V. (2022) · PROTEOMICS · doi:10.1002/pmic.202200074 · Cited by 28 · see citing works

A cryptic K48 ubiquitin chain binding site on UCH37 is required for its role in proteasomal degradation

Du, J., Babik, S., Li, Y., Deol, K. K., Eyles, S. J., Fejzo, J., Tonelli, M., & Strieter, E. R. (2022) · eLife · doi:10.7554/elife.76100 · Cited by 30 · see citing works

Human genetic defects in SRP19 and SRPRA cause severe congenital neutropenia with distinctive proteome changes

Linder, M. I., Mizoguchi, Y., Hesse, S., Csaba, G., Tatematsu, M., Łyszkiewicz, M., Ziętara, N., Jeske, T., Hastreiter, M., Rohlfs, M., et al. (2022) · Blood · doi:10.1182/blood.2022016783 · Cited by 31 · see citing works

Ubiquitin Signaling Regulates RNA Biogenesis, Processing, and Metabolism

Thapa, P. S., Shanmugam, N., & Pokrzywa, W. (2019) · BioEssays · doi:10.1002/bies.201900171 · Cited by 29 · see citing works

Functional impacts of the ubiquitin–proteasome system on DNA damage recognition in global genome nucleotide excision repair

Sakai, W., Yuasa‐Sunagawa, M., Kusakabe, M., Kishimoto, A., Matsui, T., Kaneko, Y., Akagi, J., Huyghe, N. D., Ikura, M., Ikura, T., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-76898-2 · Cited by 28 · see citing works

From the Evasion of Degradation to Ubiquitin-Dependent Protein Stabilization

Ahmad, Y. A., Oknin-Vaisman, A., Bitman-Lotan, E., & Orian, A. (2021) · Cells · doi:10.3390/cells10092374 · Cited by 26 · see citing works

K27‐linked ubiquitylation promotes p97 substrate processing and is essential for cell proliferation

Shearer, R. F., Typas, D., Coscia, F., Schovsbo, S. U., Kruse, T., Mund, A., & Mailand, N. (2022) · The EMBO Journal · doi:10.15252/embj.2021110145 · Cited by 29 · see citing works

HSP70-binding motifs function as protein quality control degrons

Abildgaard, A. B., Voutsinos, V., Petersen, S. D., Larsen, F. B., Kampmeyer, C., Johansson, K. E., Stein, A., Ravid, T., Andréasson, C., Jensen, M. K., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04679-3 · Cited by 29 · see citing works

Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions

Mirsanaye, A. S., Typas, D., & Mailand, N. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.01.008 · Cited by 28 · see citing works

The ubiquitination code: a signalling problem

Woelk, T., Sigismund, S., Penengo, L., & Polo, S. (2007) · Cell Division · doi:10.1186/1747-1028-2-11 · Cited by 140 · see citing works

The increasing complexity of the ubiquitin code

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

Post-translational regulation of ubiquitin signaling

Song, L., & Luo, Z. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902074 · Cited by 340 · see citing works

E3 Ligase-Mediated Protein Quality Control Mechanisms: Insights into Maintaining Cellular Integrity Across Pluripotency, Cancer, and Neurodegeneration

Kolla, S. (2024) · eScholarship (California Digital Library)

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 608 · see citing works