Themes and variations on ubiquitylation

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024

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

RING Finger Proteins

Joazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249

Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

Zhang, Y., Gao, J., Chung, K. K. K., Huang, H., Dawson, V. L., & Dawson, T. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240347797 · Cited by 982

Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53

Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724

The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families

Kamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Conaway, R. C., & Conaway, J. W. (1998) · Genes & Development · doi:10.1101/gad.12.24.3872 · Cited by 595

Nedd8 Modification of Cul-1 Activates SCFβTrCP-Dependent Ubiquitination of IκBα

Read, M. A., Brownell, J. E., Gladysheva, T. B., Hottelet, M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R.-S., Chau, V., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2326-2333.2000 · Cited by 363

MDM2 suppresses p73 function without promoting p73 degradation

Zeng, X., Chen, L., Jost, C. A., Maya, R., Keller, D., Wang, X., Kaelin, W. G., Oren, M., Chen, J., & Lu, H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3257 · Cited by 334

MdmX Protects p53 from Mdm2-Mediated Degradation

Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211

Harnessing the Ubiquitination Machinery to Target the Degradation of Specific Cellular Proteins

Zhou, P., Bogacki, R., McReynolds, L., & Howley, P. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00074-5 · Cited by 164

IAP proteins: blocking the road to death's door

Salvesen, G. S., & Duckett, C. S. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm830 · Cited by 1,756

Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation

Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P., & Dikic, I. (2003) · Nature Cell Biology · doi:10.1038/ncb983 · Cited by 715

CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein

Murata, S., Minami, Y., Minami, M., Chiba, T., & Tanaka, K. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve246 · Cited by 574

Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity

Xirodimas, D. P., Saville, M. K., Bourdon, J.-C., Hay, R. T., & Lane, D. P. (2004) · Cell · doi:10.1016/j.cell.2004.06.016 · Cited by 570

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

Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression

Colledge, M., Snyder, E. M., Crozier, R. A., Soderling, J. A., Jin, Y., Langeberg, L. K., Lu, H., Bear, M. F., & Scott, J. D. (2003) · Neuron · doi:10.1016/s0896-6273(03)00687-1 · Cited by 567

Myocytes Die by Multiple Mechanisms in Failing Human Hearts

Kostin, S., Pool, L., Elsässer, A., Hein, S., Drexler, H. C. A., Arnon, E., Hayakawa, Y., Zimmermann, R., Bauer, E., Klövekorn, W.-P., et al. (2003) · Circulation Research · doi:10.1161/01.res.0000067471.95890.5c · Cited by 564

Coping with stress: multiple ways to activate p53

Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522

The F-Box Protein Skp2 Participates in c-Myc Proteosomal Degradation and Acts as a Cofactor for c-Myc-Regulated Transcription

von der Lehr, N., Johansson, S., Wu, S., Bahram, F., Castell, A., Cetinkaya, C., Hydbring, P., Weidung, I., Nakayama, K., Nakayama, K. I., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00193-x · Cited by 408

Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG-CoA reductase

DeBose-Boyd, R. A. (2008) · Cell Research · doi:10.1038/cr.2008.61 · Cited by 391

p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria

Okatsu, K., Saisho, K., Shimanuki, M., Nakada, K., Shitara, H., Sou, Y., Kimura, M., Sato, S., Hattori, N., Komatsu, M., et al. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01426.x · Cited by 397

The Cbl interactome and its functions

Schmidt, M. H. H., & Dikic, I. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1762 · Cited by 395

Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications

Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395

CARMA1, BCL-10 and MALT1 in lymphocyte development and activation

Thome, M. (2004) · Nature Reviews Immunology · doi:10.1038/nri1352 · Cited by 391

Human HRD1 Is an E3 Ubiquitin Ligase Involved in Degradation of Proteins from the Endoplasmic Reticulum

Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384

Distinct monoubiquitin signals in receptor endocytosis

Haglund, K. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.005 · Cited by 367

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53

Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346

Sorting of proteins into multivesicular bodies: ubiquitin‐dependent and ‐independent targeting

Reggiori, F., & Pelham, H. R. B. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5176 · Cited by 324

Targeting proteins for degradation.

Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287

Endocytosis of Receptor Tyrosine Kinases Is Driven by Monoubiquitylation, Not Polyubiquitylation

Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J., & Yarden, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300096200 · Cited by 286

The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate

Dentice, M., Bandyopadhyay, A., Gereben, B., Callebaut, I., Christoffolete, M. A., Kim, B. W., Nissim, S., Mornon, J.-P., Zavacki, A. M., Zeöld, A., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1272 · Cited by 227

E3 ubiquitin ligases as T cell anergy factors

Mueller, D. L. (2004) · Nature Immunology · doi:10.1038/ni1106 · Cited by 224

Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system

Wang, X., Fan, H., Ying, Z., Li, B., Wang, H., & Wang, G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.055 · Cited by 207

E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation

d'Azzo, A., Bongiovanni, A., & Nastasi, T. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00294.x · Cited by 206

Identification of the ubiquitin–protein ligase that recognizes oxidized IRP2

Yamanaka, K., Ishikawa, H., Megumi, Y., Tokunaga, F., Kanie, M., Rouault, T. A., Morishima, I., Minato, N., Ishimori, K., & Iwai, K. (2003) · Nature Cell Biology · doi:10.1038/ncb952 · Cited by 181

Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network

Markson, G., Kiel, C., Hyde, R., Brown, S., Charalabous, P., Bremm, A., Semple, J., Woodsmith, J., Duley, S., Salehi-Ashtiani, K., et al. (2009) · Genome Research · doi:10.1101/gr.093963.109 · Cited by 157

Stabilization of the E3 Ubiquitin Ligase Nrdp1 by the Deubiquitinating Enzyme USP8

Wu, X., Yen, L., Irwin, L., Sweeney, C., & Carraway, K. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7748-7757.2004 · Cited by 144

S -nitrosoprotein formation and localization in endothelial cells

Yang, Y., & Loscalzo, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405989102 · Cited by 141

Ubiquitin. Not just for proteasomes anymore

Aguilar, R. C., & Wendland, B. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00010-3 · Cited by 138

NARF, an Nemo-like Kinase (NLK)-associated Ring Finger Protein Regulates the Ubiquitylation and Degradation of T Cell Factor/Lymphoid Enhancer Factor (TCF/LEF)

Yamada, M., Ohnishi, J., Ohkawara, B., Iemura, S., Satoh, K., Hyodo-Miura, J., Kawachi, K., Natsume, T., & Shibuya, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602089200 · Cited by 132

Impact of ageing on proteasome structure and function in human lymphocytes

Carrard, G., Dieu, M., Raes, M., Toussaint, O., & Friguet, B. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00356-4 · Cited by 131

Simian Virus 5 V Protein Acts as an Adaptor, Linking DDB1 to STAT2, To Facilitate the Ubiquitination of STAT1

Precious, B., Childs, K., Fitzpatrick-Swallow, V., Goodbourn, S., & Randall, R. E. (2005) · Journal of Virology · doi:10.1128/jvi.79.21.13434-13441.2005 · Cited by 117

Control of biochemical reactions through supramolecular RING domain self-assembly

Kentsis, A., Gordon, R. E., & Borden, K. L. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202608799 · Cited by 112

A proteomics approach to identify the ubiquitinated proteins in mouse heart

Jeon, H. B., Choi, E. S., Yoon, J. H., Hwang, J. H., Chang, J. W., Lee, E. K., Choi, H. W., Park, Z.-Y., & Yoo, Y. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.015 · Cited by 101

An Atypical E3 Ligase Zinc Finger Protein 91 Stabilizes and Activates NF-κB-inducing Kinase via Lys63-linked Ubiquitination

Jin, X., Jin, H. R., Jung, H. S., Lee, S. J., Lee, J.-H., & Lee, J. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129551 · Cited by 94

The ubiquitin proteasome system in synaptic and axonal degeneration

Korhonen, L., & Lindholm, D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311091 · Cited by 72

Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination

Xie, F., Zhang, Z., Van Dam, H., Zhang, L., & Zhou, F. (2014) · Cells · doi:10.3390/cells3040981 · Cited by 70

Ubiquitination and Proteasomal Degradation of Endogenous and Exogenous Inositol 1,4,5-Trisphosphate Receptors in αT3-1 Anterior Pituitary Cells

Wojcikiewicz, R. J. H., Xu, Q., Webster, J. M., Alzayady, K., & Gao, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206607200 · Cited by 63

In vitro and in vivo specificity of ubiquitination and degradation of STAT1 and STAT2 by the V proteins of the paramyxoviruses simian virus 5 and human parainfluenza virus type 2

Precious, B., Young, D. F., Andrejeva, L., Goodbourn, S., & Randall, R. E. (2005) · Journal of General Virology · doi:10.1099/vir.0.80263-0 · Cited by 56

Structural and Functional Comparison of the RING Domains of Two p53 E3 Ligases, Mdm2 and Pirh2

Shloush, J., Vlassov, J. E., Engson, I., Duan, S., Saridakis, V., Dhe-paganon, S., Raught, B., Sheng, Y., & Arrowsmith, C. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157669 · Cited by 42

Endotoxin reduces CD95-induced neutrophil apoptosis by cIAP-2-mediated caspase-3 degradation

Mica, L., Härter, L., Trentz, O., & Keel, M. (2004) · Journal of the American College of Surgeons · doi:10.1016/j.jamcollsurg.2004.05.272 · Cited by 40

Structure of the human UBR5 E3 ubiquitin ligase

Wang, F., He, Q., Zhan, W., Yu, Z., Finkin-Groner, E., Ma, X., Lin, G., & Li, H. (2023) · Structure · doi:10.1016/j.str.2023.03.010 · Cited by 39

Genome-Wide Analysis Identifies MYND-Domain Protein Mub1 as an Essential Factor for Rpn4 Ubiquitylation

Ju, D., Wang, X., Xu, H., & Xie, Y. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01787-07 · Cited by 38

Functional connections between cell cycle and proteostasis in the regulation of Candida albicans morphogenesis

Hossain, S., Lash, E., Veri, A. O., & Cowen, L. E. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108781 · Cited by 31

Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity

Zhou, X., Zhang, H., Wang, Y., Wang, D., Lin, Z., Zhang, Y., Tang, Y., Liu, J., Yao, Y.-F., Zhang, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58432-y · Cited by 17