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

Accumulation of dually targeted StGPT1 in chloroplasts mediated by StRFP1, an E3 ubiquitin ligase, enhances plant immunity

Wu, X., Zhou, X., Lin, T., Zhang, Z., Wu, X., Zhang, Y., Liu, Y., & Tian, Z. (2024) · Horticulture Research · doi:10.1093/hr/uhae241 · Cited by 7

Dual functionality of MDM2 in PROTACs expands the horizons of targeted protein degradation

Zhao, J., Chen, H., & Liang, C. (2025) · Biomarker Research · doi:10.1186/s40364-025-00826-7 · Cited by 7

Reprogramming SUMO-primed ubiquitylation: opportunities in oncology and neurology

Gotthardt, G., Keiten‐Schmitz, J., & Müller, S. P. (2025) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2025.09.002 · Cited by 7

Secondary interactions in ubiquitin-binding domains achieve linkage or substrate specificity

Michel, M. A., Scutts, S. R., & Komander, D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114545 · Cited by 8

Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes

Swarnkar, A., Leidner, F., Rout, A. K., Ainatzi, S., Schmidt, C. C., Becker, S., Urlaub, H., Griesinger, C., Grubmüller, H., & Stein, A. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00301-3 · Cited by 7

Distinct Stress Regulators in the CRL Family: Emerging Roles of F‐Box Proteins

Hwang, J., Lauinger, L., & Kaiser, P. (2025) · BioEssays · doi:10.1002/bies.202400249 · Cited by 7

Structural diversity and oligomerization of bacterial ubiquitin-like proteins

Gong, M., Ye, Q., Gu, Y., Chambers, L. R., Bobkov, A. A., Arakawa, N. K., Matyszewski, M., & Corbett, K. D. (2025) · Structure · doi:10.1016/j.str.2025.03.011 · Cited by 7

Mass Spectrometry‐Based Analysis of Time‐Resolved Proteome Quantification

Valdés, A., & Lind, S. B. (2019) · PROTEOMICS · doi:10.1002/pmic.201800425 · Cited by 7

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 · doi:10.1002/ange.202105870 · Cited by 7

In silico analysis of the profilaggrin sequence indicates alterations in the stability, degradation route, and intracellular protein fate in filaggrin null mutation carriers

Paul, A. A., Szulc, N. A., Kobiela, A., Brown, S., Pokrzywa, W., & Gutowska‐Owsiak, D. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1105678 · Cited by 8

Chromatin targeting of the RNF12/RLIM E3 ubiquitin ligase controls transcriptional responses

Espejo-Serrano, C., Aitken, C., Tan, B. F., May, D. G., Chrisopulos, R. J., Roux, K. J., Demmers, J., Mackintosh, S. G., Gribnau, J. H., Bustos, F., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202302282 · Cited by 8

A ligand discovery toolbox for the WWE domain family of human E3 ligases

Münzker, L., Kimani, S., Fowkes, M. M., Dong, A., Zheng, H., Li, Y., Dasovich, M., Żak, K. M., Leung, A. K. L., Elkins, J. M., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06584-w · Cited by 7

Studying the ubiquitin code through biotin-based labelling methods

Barroso‐Gomila, O., Muratore, V., Merino‐Cacho, L., Rodríguez, J. A., Barrio, R., & Sutherland, J. D. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.009 · Cited by 6

Linkage‐Specific Synthesis of Di‐ubiquitin Probes Enabled by the Incorporation of Unnatural Amino Acid ThzK

Zhou, H., Carpenter, T., Fu, X., Jin, B., Ody, B. K., Hassan, M. S., Jacobs, S. E., Cheung, J. W., Nicholson, E. M., Turlington, M., et al. (2022) · ChemBioChem · doi:10.1002/cbic.202200133 · Cited by 6

Mechanically transduced immunosorbent assay to measure protein-protein interactions

Petell, C. J., Randene, K., Pappas, M., Sandoval, D., Strahl, B. D., Harrison, J. S., & Steimel, J. P. (2021) · eLife · doi:10.7554/elife.67525 · Cited by 7

Tools for Decoding Ubiquitin Signaling in DNA Repair

Foster, B., Attwood, M., & Gibbs‐Seymour, I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.760226 · Cited by 5

The F-box protein ZmFBK1 facilitates autophagy-mediated degradation of maize NLR protein Rp1-D21 to suppress the hypersensitive response

Tang, C.-X., Ma, S.-J., Ge, Q.-D., Sun, Y., Liu, T., Yang, M., Kang, Z.-X., Dai, Y.-C., Zhang, X., Liu, X., et al. (2026) · Molecular Plant · doi:10.1016/j.molp.2026.01.001 · Cited by 5

UBE2J1 Suppresses Colorectal Cancer Progression via Ubiquitin-Mediated Degradation of RPS3

Rivas, D. S., & Molina, P. A. (2025) · Archive of International Journal of Cancer and Allied Science · doi:10.51847/7ubioajlao · Cited by 5

Avidity-based biosensors for ubiquitylated PCNA reveal choreography of DNA damage bypass

Yakoub, G., Choi, Y., Wong, R. P. C., Strauch, T., Ann, K. J., Cohen, R. E., & Ulrich, H. D. (2023) · Science Advances · doi:10.1126/sciadv.adf3041 · Cited by 5

APC/C-mediated ubiquitylation of extranucleosomal histone complexes lacking canonical degrons

Skrajna, A., Bodrug, T., Martinez‐Chacin, R. C., Fisher, C. B., Welsh, K. A., Simmons, H. C., Arteaga, E. C., Simmons, J. M., Nasr, M. A., LaPak, K. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57384-7 · Cited by 5

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 · doi:10.1002/ange.202002974 · Cited by 5

The Arabidopsis thaliana E3 Ubiquitin Ligase BRIZ Functions in Abscisic Acid Response

Linden, K. J., Hsia, M. M., Chen, Y., & Callis, J. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.641849 · Cited by 5

The role of ubiquitin signaling pathway on liver regeneration in rats

Yaylacı, A. Ö., & Canbek, M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04482-5 · Cited by 6

Single-Molecule and Vesicle Trafficking Analysis of Ubiquitination Involved in the Activity of Ammonium Transporter AMT1;3 in Arbidopsis under High Ammonium Stress

Zhao, R., Cao, Y., Ge, Y., Xu, J., Li, R., Yang, M., Chen, Y., Wu, D., Xiao, J., & Li, R. (2022) · Cells · doi:10.3390/cells11223651 · Cited by 5

Deubiquitinating enzyme PSMD7 promotes bladder cancer development: Involvement of RAB1A stabilization

Wang, J., Wang, T., Feng, Y., Liu, Y., Fu, B., Liu, X., & Wu, Q.-Z. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110996 · Cited by 5

Design of bifunctional molecules to accelerate post-translational modifications: achievements and challenges

Wang, Y., He, Y., You, Q., & Wang, L. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104194 · Cited by 5

Mechanistic basis for protein conjugation in a diverged bacterial ubiquitination pathway

Ye, Q., Gong, M., Cai, J., Chambers, L. R., Zhou, H., Suhandynata, R. T., & Corbett, K. D. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01696-1 · Cited by 5

The E3 ubiquitin ligase mindbomb1 controls planar cell polarity-dependent convergent extension movements during zebrafish gastrulation

Saraswathy, V. M., Sharma, P., Kurup, A. J., Polès, S., Poulain, M., & Fürthauer, M. (2022) · eLife · doi:10.7554/elife.71928 · Cited by 5

Acyl azide modification of the ubiquitin C-terminus enables DUB capture

Xiao, H., Guo, Y., Wang, Y., Chu, G., Li, P., & Shi, J. M. (2022) · Chemical Communications · doi:10.1039/d2cc06496k · Cited by 5

Mechanisms and Design Principles of Proteolysis-Targeting Chimeras and Their Emerging Applications

Knoll, N., Neamati, N., & Üren, A. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00730 · Cited by 5

Unique gluing effect of ASXL1 K351 monoubiquitination stimulates the PR-DUB activity

Zhang, T., Zheng, J., Tong, Z., Deng, Z., He, Z., Wu, X., Wang, M., Du, Y., Xu, Z., Tao, S., et al. (2026) · Nature Chemical Biology · doi:10.1038/s41589-025-02126-5 · Cited by 4

Involvement of E3 Ubiquitin Ligases in Viral Infections of the Human Host

Verma, S., & Ghatak, A. (2024) · Viral Immunology · doi:10.1089/vim.2024.0068 · Cited by 4

Tom40 functions as a channel for protein retrotranslocation in the mitochondria-associated degradation (MAD) pathway

Liao, P., Lin, T., Tsang, C. A., Huang, C.-H., Filpo, K., Boldogh, I. R., & Pon, L. A. (2025) · Communications Biology · doi:10.1038/s42003-025-08549-z · Cited by 4

A Mass Spectrometry-Based Strategy for Mapping Modification Sites for the Ubiquitin-Like Modifier NEDD8

Oliveira, C. A. B., Isaakova, E. A., Beli, P., & Xirodimas, D. P. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2859-1_10 · Cited by 4

Loss of the deubiquitinase OTULIN promotes hepatocellular carcinoma (HCC) in an mTOR-dependent manner

Marzio, A., & Pagano, M. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0531-2 · Cited by 4

Bacterial antiviral defense pathways encode eukaryotic-like ubiquitination systemsPreprint

Chambers, L. R., Ye, Q., Cai, J., Gong, M., Ledvina, H. E., Zhou, H., Whiteley, A. T., Suhandynata, R. T., & Corbett, K. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.26.559546 · Cited by 4

Phase Separation Clustering of Poly Ubiquitin Cargos on Ternary Mixture Lipid Membranes by Synthetically Cross-Linked Ubiquitin Binder Peptides

Kim, S. J., Okafor, K. K., Tabuchi, R., Briones, C., & Lee, I. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00483 · Cited by 3

UBE2S inhibits colorectal cancer proliferation by regulating the PI3K/AKT and MAPK/ERK pathways via TRAF6

Li, J., Feng, H., Liu, K., Huang, H., Ji, X., Zhang, T., Cheng, X., & Zhao, R. (2025) · Scientific Reports · doi:10.1038/s41598-025-18637-z · Cited by 3

Cysteine-reactive covalent chloro-N-acetamide ligands induce ferroptosis mediated cell death

Gotthardt, G., Weckesser, J., Tascher, G., da Gama, S. B., Uckelmann, H. J., Sun, S., Schwalm, M. P., Mosler, T., Ferrario, G., Angeli, J. P. F., et al. (2025) · EMBO Reports · doi:10.1038/s44319-025-00593-4 · Cited by 3

Linear poly-ubiquitin remodels the proteome and influences hundreds of regulators in Drosophila

Nuga, O., Richardson, K., Patel, N. C., Wang, X., Pagala, V., Stephan, A., Peng, J., Demontis, F., & Todi, S. V. (2024) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkae209 · Cited by 3

The E3 ubiquitin ligase Nedd4 fosters developmental myelination in the mouse central and peripheral nervous system

Fimiani, C., Pereira, J. A., Gerber, J., Berg, I., DeGeer, J., Bachofner, S., Fischer, J. S., Kauffmann, M., & Suter, U. (2024) · Glia · doi:10.1002/glia.24642 · Cited by 3

Research and development prospects of TRIM65

Deng, N.-H., Chen, J.-H., Tian, Z., & Quan, S.-B. (2025) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-025-06285-9 · Cited by 3

High-Content RNAi Phenotypic Screening Unveils the Involvement of Human Ubiquitin-Related Enzymes in Late Cytokinesis

Boullé, M., Davignon, L., Halidi, K. N. S., Guez, S., Giraud, É., Hollenstein, M., & Agou, F. (2022) · Cells · doi:10.3390/cells11233862 · Cited by 3

Fraternity of old‐timers: How ubiquitin regulates miRNA functions

Ryazansky, S. S., & Akulenko, N. V. (2023) · BioEssays · doi:10.1002/bies.202200220 · Cited by 4

Ubiquitin: Not just a one‐way ticket to the proteasome, but a therapeutic dial to fine‐tune the molecular landscape of disease

Kim, A. H., Chiknas, P. M., & Lee, R. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1769 · Cited by 3

UBR1 promotes anaplastic thyroid carcinoma progression via stabilizing YAP through monoubiquitylation

Xia, M., Chen, L., Yu, Y., Luo, J., Zeng, Y., Zhang, M., Tang, J., Jiang, Z., Gong, Y., & Xie, C. (2024) · Scientific Reports · doi:10.1038/s41598-024-70458-8 · Cited by 3

Localized K63 Ubiquitin Signaling Is Regulated by VCP/p97 During Oxidative Stress

Maduka, A. O., Manohar, S., Foster, M. W., & Silva, G. M. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100920 · Cited by 4

“Pupdates” on proteasomal degradation in bacteria

Kahne, S. C., & Darwin, K. H. (2025) · Journal of Bacteriology · doi:10.1128/jb.00111-25 · Cited by 3

Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry

Shestoperova, E. I., Ivanov, D. G., & Strieter, E. R. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00016 · Cited by 3

Regulation of human development by ubiquitin chain editing of chromatin remodelersPreprint

Beck, D. B., Basar, M. A., Asmar, A. J., Thompson, J. J., Oda, H., Uehara, D. T., Saida, K., D’Souza, P., Bodurtha, J. N., Mu, W., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.23.917450 · Cited by 3

Oligomerization-driven MLKL ubiquitylation antagonises necroptosisPreprint

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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.01.442209 · Cited by 3

Induced polyubiquitination of proteins mediated by overexpression of a peptide: a novel tool for targeted protein degradation (TPD) research.Preprint

Nallur, G. (2022) · Research Square · doi:10.21203/rs.3.rs-1547607/v1 · Cited by 3

NEMO reshapes the protein aggregate interface and promotes aggrephagy by co-condensation with p62Preprint

Furthmann, N., Angersbach, L., Bader, V., Blusch, A., Goel, S., Sánchez‐Vicente, A., Krause, L. J., Grover, P. L., Trinkaus, V. A., van Well, E. M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.05.543428 · Cited by 3

Rhizophagus irregularis DAOM197198 modulates the root ubiquitinome of Medicago truncatula in the establishment and functioning of arbuscular mycorrhizal symbiosis

Inès, D., Pichereaux, C., Wendehenne, D., Courty, P., & Rosnoblet, C. (2025) · Mycorrhiza · doi:10.1007/s00572-025-01226-3 · Cited by 2

Drosophila proteasome subunit Rpn8 controls IMD pathway activation via PGRP-SC2 degradation

Wu, M., Ali, U., Ding, S., Zhang, C., Jin, Y., Cao, X., Saeed, M. A. R., Zhu, Y., Usama, M., Raza, B., et al. (2025) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2025.104422 · Cited by 2

Modulation of the tumor microenvironment by the ubiquitin–proteasome system in colorectal cancer

Wang, X., Ren, Y., Song, R., Liu, J., Zhou, Y., Yang, S., Liu, Y., Lei, Y., & Zhao, X. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07487-y · Cited by 3

Encoding and decoding ubiquitin chain architectures: fine-tuning the fate of proteins

Tomomatsu, S., & Ohtake, F. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf075 · Cited by 3

Advances in the diagnosis and treatment of oligoasthenozoospermia based on epigenetic regulation

Zhao, H.-B., Ba, W.-Y., Zhu, W.-B., Wang, G.-Z., Wang, Z.-L., & Wang, S. (2026) · Therapeutic Advances in Urology · doi:10.1177/17562872251414924 · Cited by 2

The ubiquitin‐proteasome system and autophagy as guardians of the cellular proteome

Đikić, I. (2026) · FEBS Letters · doi:10.1002/1873-3468.70371 · Cited by 4

Diverse ubiquitin codes in the regulation of inflammatory signaling

Ikeda, F. (2020) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.96.032 · Cited by 2

Sequential release of interacting proteins and Ub-modifying enzymes by disulfide heterotypic ubiquitin reagents

Cai, H., Wu, X., Mao, J., Tong, Z., Yan, D., Weng, Y., & Zheng, Q. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107186 · Cited by 2

Deletion of a core APC/C component reveals APC/C function in regulating neuronal USP1 levels and morphology

Day, J. L., Tirard, M., & Brose, N. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1352782 · Cited by 2

The biogenesis of potassium transporters: implications of disease-associated mutations

Kok, M., & Brodsky, J. L. (2024) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2024.2369986 · Cited by 2

FBXL6 is a vulnerability in AML and unmasks proteolytic cleavage as a major experimental pitfall in myeloid cells

Sperk, A., Gabriel, A., Koch, D., Augsburger, A., Sanchez, V., Brockelt, D., Öllinger, R., Engleitner, T., Giansanti, P., Ludwig, R., et al. (2024) · Leukemia · doi:10.1038/s41375-024-02345-0 · Cited by 2

Rapid clinical deployment of UBA1 testing in patients with VEXAS syndrome

Wadsworth, P. A., Chen, S., Lawrence, L., Ho, C. C., Le, J. E., Libiran, P., Grayson, P. C., Ferrada, M. A., Beck, D. B., & Suarez, C. J. (2025) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqaf051 · Cited by 2

Mechanisms of USP18 specificity toward ISG15 revealed by paralog sequence analysis comparison

Bonacci, T., Bolhuis, D. L., Brown, N. G., & Emanuele, M. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110288 · Cited by 2

Fbxo2 inhibits cell proliferation, migration and invasion by the ubiquitin-mediated degradation of WEE1 in renal cell carcinoma

Wang, L., Zang, Y., Yang, C., Xu, M., Dai, G., Xiang, H., Ma, J., Wang, Z. P., Liu, X., & Xue, B. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01091-4 · Cited by 2

Quantitative Proteomics Combined with Two Genetic Strategies for Screening Substrates of Ubiquitin Ligase Hrt3

Lan, Q., Wang, Y., Sun, Z., Li, Y., Zhang, C., Chang, L., Gao, Y., Wu, J., Wang, F., & Xu, P. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00673 · Cited by 2

What the genes tell us in the VEXAS syndrome? A rheumatologist's perspective

Kobak, Ş. (2023) · International Journal of Rheumatic Diseases · doi:10.1111/1756-185x.14646 · Cited by 2

Prediction of Plant Ubiquitylation Proteins and Sites by Fusing Multiple Features

Guan, M.-Y., Wang, Q., Wu, P., Qiu, W., Yu, W., & Xiao, X. (2023) · Current Bioinformatics · doi:10.2174/1574893618666230908092847 · Cited by 2

A RNF12-USP26 amplification loop promotes germ cell specification and is disrupted in urogenital disordersPreprint

Segarra-Fas, A., Bustos, F., Toth, R. L., Nardocci, G., & Findlay, G. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.16.378398 · Cited by 2

Zebrafish Nedd8 Facilitates Ovarian Development and the Maintenance of Female Secondary Sexual Characteristics Via Suppression of Androgen Receptor ActivityPreprint

Yu, G., Liu, X., Zhang, D., Wang, J., Ouyang, G., Chen, Z., & Xiao, W. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3323376 · Cited by 2

Specific genomic targeting of the RNF12/RLIM E3 ubiquitin ligase selectively programmes developmental transcriptionPreprint

Espejo-Serrano, C., Aitken, C., Tan, B. F., May, D. G., Chrisopulos, R. J., Roux, K. J., Mackintosh, S. G., Gribnau, J. H., Bustos, F., Gontan, C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.14.544957 · Cited by 2

CDK/mTOR–dependent phosphorylation of UBE2H restrains its charging with ubiquitin and regulates CTLH-dependent degradationPreprint

Chen, Y., Rossio, V., Paulo, J. A., Karki, M., Manohar, S., Ozimek, N., Frizzi, L., Gygi, S. P., & King, R. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.07.710281 · Cited by 2

Targeting USP14/UCHL5: A Breakthrough Approach to Overcoming Treatment-Resistant FLT3-ITD-Positive AML

Nogami, A., Amemiya, H. J., Fujiwara, H., Umezawa, Y., Tohda, S., & Nagao, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910372 · Cited by 1

Semi-synthesis of functionalized cell-permeable ubiquitin probes via SrtA-mediated ligation

Liu, L., Wang, B., Yang, S., Wang, W., Wang, Y., & Li, Y.-M. (2025) · Organic & Biomolecular Chemistry · doi:10.1039/d5ob00261c · Cited by 1

Functional Characterization of Deubiquitinase UBP Family and Proteomic Analysis of Aaubp14-Mediated Pathogenicity Mechanism in Alternaria alternata

Tang, J., Zhou, H., Jiao, C., & Li, H. (2025) · Journal of Fungi · doi:10.3390/jof11070495 · Cited by 1

DIG-DUBs: mechanisms and functions of ISG15 deconjugation by human and viral cross-reactive ubiquitin proteases

Bonacci, T., & Emanuele, M. J. (2025) · Biochemical Society Transactions · doi:10.1042/bst20240859 · Cited by 3

Ubiquitination of Metabotropic Glutamate Receptors and Associated Synaptic Proteins In Vitro and In Vivo

Mao, L., & Wang, J. Q. (2026) · Journal of Cellular Signaling · doi:10.33696/signaling.6.145 · Cited by 1

Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis

Darwin, K. H. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111373 · Cited by 1

Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts

Lau, A. S., Nellaepalli, S., & Jarvis, P. (2026) · Nature Communications · doi:10.1038/s41467-026-74728-z · Cited by 2

YME1L1 degradation by TRIM21 inhibits bladder cancer proliferation, metastasis, and mitochondrial function

Sun, L., Yao, Y., Gong, S., 陈政良, Xie, W., Wang, L., & Liu, X. (2026) · Oncogene · doi:10.1038/s41388-026-03903-9 · Cited by 1

MALDI-TOF Mass Spectrometry for interrogating ubiquitin enzymes

Cesare, V. D. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1184934 · Cited by 1

In vivo RNAi screening identifies multiple deubiquitinases required for the maintenance of intestinal homeostasis in Drosophila

Zhao, B., Luo, J., Wang, H., Li, Y., Li, D., & Li, D. (2024) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2024.104162 · Cited by 1

Application of chemical protein synthesis in the study of protein ubiquitination

Wu, S., Liang, J., Wu, X., Deng, Z., & Liu, L. (2024) · Scientia Sinica Chimica · doi:10.1360/ssc-2024-0225 · Cited by 2

Detection of ubiquitinated targets in mammalian and Drosophila models

Maspero, E., Fajner, V., Weber, J., & Polo, S. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.030 · Cited by 1

Resistance to Proteasome Inhibitor Therapy in Non-Hodgkin Lymphoma

Miles, R. R., & Galardy, P. J. (2019) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-030-24424-8_4 · Cited by 1

Studying OTUD6B-OTUB1 Protein–Protein Interaction by Low-Throughput GFP-Trap Assays and High-Throughput AlphaScreen Assays

Weber, E., Schorpp, K., & Hadian, K. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1186-9_23 · Cited by 1

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

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Influenza virus strategies to regulate S1P-metabolizing enzymes and evade host innate immunity for robust viral replication

Wolf, J. (2021) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/91025 · Cited by 1

Linear ubiquitin chains remodel the proteome and influence the levels of hundreds of regulators in DrosophilaPreprint

Nuga, O., Richardson, K., Patel, N. C., Wang, X., Pagala, V., Stephan, A., Peng, J., Demontis, F., & Todi, S. V. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.09.593206 · Cited by 1

Mechanisms of USP18 deISGylation revealed by comparative analysis with its human paralog USP41Preprint

Bonacci, T., Bolhuis, D. L., Brown, N. G., & Emanuele, M. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.28.596309 · Cited by 1

Distinct modes of coupling between VCP, an essential unfoldase, and deubiquitinasesPreprint

Vostal, L. E., Dahan, N. E., Zhang, W., Reynolds, M. J., Chait, B. T., & Kapoor, T. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.08.611915 · Cited by 1

A Protein Engineering Approach for Uncovering Cryptic Ubiquitin-binding Sites: from a Ubiquitin-Variant Inhibitor of APC/C to K48 Chain BindingPreprint

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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/669846

Neurodevelopment: UNC-40/DCC and the Patterning of Neural Circuits

Wadsworth, W. G. (2020) · Current Biology · doi:10.1016/j.cub.2020.08.102

Linear ubiquitin chains break blood vessel branches

Shibata, Y., & Komander, D. (2021) · Cell Research · doi:10.1038/s41422-021-00553-2

Chemical Damage to mRNA and Its Impact on Ribosome Quality-Control and Stress-Response Pathways in Eukaryotic Cells

Yan, L. L. (2021) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/tmky-z553

In memoriam: Huib Ovaa, the brain behind the formula (18/12/1973–19/05/2020)

Barrio, R., & Rodríguez, M. S. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.06.011

Present and Future Opportunities in Imaging the Ubiquitin System (Ub-System)

Mortati, L., Pergolizzi, B., Panuzzo, C., & Bracco, E. (2022) · Biophysica · doi:10.3390/biophysica2030018

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