Principles of Ubiquitin-Dependent Signaling

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

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

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

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

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944

The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy

Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125

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

Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872

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

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 1,474

Cellular quality control by the ubiquitin–proteasome system and autophagy

Pohl, C., & Dikic, I. (2019) · Science · doi:10.1126/science.aax3769 · Cited by 1,212

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 680

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

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

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 426

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 404

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 366

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 249

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 242

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 215

A Cellular Mechanism to Detect and Alleviate Reductive Stress

Manford, A. G., Rodríguez-Pérez, F., Shih, K. Y., Shi, Z., Berdan, C. A., Choe, M., Titov, D. V., Nomura, D. K., & Rapé, M. (2020) · Cell · doi:10.1016/j.cell.2020.08.034 · Cited by 203

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 208

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 191

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 152

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 148

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 147

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 141

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

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 137

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

Cao, Y., Xie, L., Shi, F., Tang, M., Li, Y., Hu, J., Zhao, L., Zhao, L., Yu, X., Luo, X., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00376-4 · Cited by 132

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

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 111

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 111

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 112

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 110

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 101

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

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 99

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 99

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 92

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

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

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

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 82

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

Spano, D., & Catara, G. (2023) · Cells · doi:10.3390/cells13010029 · Cited by 86

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 83

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

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

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

Zhang, J., Pan, W., Zhang, Y., Tan, M.-Y., Yin, Y., Li, Y.-M., Zhang, L., Han, L.-H., Bai, J.-K., Jiang, T., et al. (2022) · Theranostics · doi:10.7150/thno.77243 · Cited by 75

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 80

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 86

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

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

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

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

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 71

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 71

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 70

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 68

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 65

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 62

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

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 63

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 56

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 64

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

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

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

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

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 51

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

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 50

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 48

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 48

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

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 47

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

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

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 43

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 39

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

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 41

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 40

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

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

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 40

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

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 36

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 36

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 33

The Role of Ubiquitin in Regulating Stress Granule Dynamics

Krause, L. J., Herrera, M. G., & Winklhofer, K. F. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.910759 · Cited by 36

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

Mitochondrial control of cellular protein homeostasis

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

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

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 35

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 31

USP32-regulated LAMTOR1 ubiquitination impacts mTORC1 activation and autophagy induction

Hertel, A., Alves, L. M., Dutz, H., Tascher, G., Bonn, F., Kaulich, M., Đikić, I., Eimer, S., Steinberg, F., & Bremm, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111653 · Cited by 29

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

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 30

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 30

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

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

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

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 30

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

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

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 27

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

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 152

The increasing complexity of the ubiquitin code

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

Post-translational regulation of ubiquitin signaling

Song, L., & Luo, Z. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902074 · Cited by 345

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 621