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

A eukaryotic-like ubiquitination system in bacterial antiviral defence

Chambers, L. R., Ye, Q., Cai, J., Gong, M., Ledvina, H. E., Zhou, H., Whiteley, A. T., Suhandynata, R. T., & Corbett, K. D. (2024) · Nature · doi:10.1038/s41586-024-07730-4 · Cited by 30

Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L

Zhu, K., Chatrin, C., Suskiewicz, M. J., Aucagne, V., Foster, B., Kessler, B. M., Gibbs‐Seymour, I., Ahel, D., & Ahel, I. (2024) · EMBO Reports · doi:10.1038/s44319-024-00235-1 · Cited by 27

E3 Ubiquitin Ligases: Key Regulators of TGFβ Signaling in Cancer Progression

Sinha, A., Iyengar, P. V., & ten Dijke, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020476 · Cited by 30

SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance

Sharma, M., Fuertes, D., Pérez-Gil, J., & Lois, L. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.703795 · Cited by 28

Selective autophagy: adding precision in plant immunity

Leong, J. X., Langin, G., & Üstün, Ş. (2022) · Essays in Biochemistry · doi:10.1042/ebc20210063 · Cited by 27

Bortezomib advanced mechanisms of action in multiple myeloma, solid and liquid tumors along with its novel therapeutic applications

Alwahsh, M., Farhat, J., Talhouni, S., Hamadneh, L., & Hergenröder, R. (2022) · EXCLI journal · doi:10.17179/excli2022-5653 · Cited by 32

The characteristics of FBXO7 and its role in human diseases

Zhong, Y., Li, J., Ye, M., & Jin, X. (2022) · Gene · doi:10.1016/j.gene.2022.146972 · Cited by 25

Gastric cancer secreted miR-214-3p inhibits the anti-angiogenesis effect of apatinib by suppressing ferroptosis in vascular endothelial cells

WANG, W., Wang, T., ZHANG, Y., Deng, T., ZHANG, H., & Ba, Y. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2023.046676 · Cited by 26

Emerging Developments in Targeting Proteotoxicity in Neurodegenerative Diseases

McAlary, L., Plotkin, S. S., & Cashman, N. R. (2019) · CNS Drugs · doi:10.1007/s40263-019-00657-9 · Cited by 26

The Ubiquitin–Proteasome System (UPS) and Viral Infection in Plants

Lobaina, D. P., Tarazi, R., Castorino, T., & Vaslin, M. F. S. (2022) · Plants · doi:10.3390/plants11192476 · Cited by 27

VEXAS syndrome: Current clinical, diagnostic and treatment approaches

Kobak, Ş. (2023) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2023.01020 · Cited by 26

EphA2 in Cancer: Molecular Complexity and Therapeutic Opportunities

Toracchio, L., Carrabotta, M., Mancarella, C., Morrione, A., & Scotlandi, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212191 · Cited by 28

USP9X prevents AGEs-induced upregulation of FN and TGF-β1 through activating Nrf2-ARE pathway in rat glomerular mesangial cells

Huang, K., & Zhao, X. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112100 · Cited by 25

The OTUD6B‐LIN28B‐MYC axis determines the proliferative state in multiple myeloma

Paulmann, C., Spallek, R., Karpiuk, O., Heider, M., Schäffer, I., Zecha, J., Klaeger, S., Walzik, M., Öllinger, R., Engleitner, T., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022110871 · Cited by 24

Interferon, restriction factors and SUMO pathways

Asmi, F. E., McManus, F. P., Thibault, P., & Chelbi‐Alix, M. K. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.03.001 · Cited by 25

A bifunctional molecule-assisted synthesis of mimics for use in probing the ubiquitination system

Zheng, Q., Wang, T., Mao, J., Chu, G., Liang, L., Jing, Y., Zuo, C., Yu, Y., Hu, H., & Pan, M. (2022) · Nature Protocols · doi:10.1038/s41596-022-00761-z · Cited by 26

Epigenetic markers in the embryonal germ cell development and spermatogenesis

Odroniec, A., Olszewska, M., & Kurpisz, M. K. (2023) · Basic and Clinical Andrology · doi:10.1186/s12610-022-00179-3 · Cited by 24

Redox Regulation in Age-Related Cataracts: Roles for Glutathione, Vitamin C, and the NRF2 Signaling Pathway

Bejarano, E., Weinberg, J., Clark, M., Taylor, A., Rowan, S., & Whitcomb, E. A. (2023) · Nutrients · doi:10.3390/nu15153375 · Cited by 27

The ubiquitin proteoform problem

Deol, K. K., & Strieter, E. R. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.015 · Cited by 22

Ubiquitin proteasome system in cardiac fibrosis

Zeng, L., Zhang, X., Huang, Z., Song, S., Li, M., Wang, T., Sun, A., & Ge, J. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.12.006 · Cited by 25

Ubiquitin-dependent translation control mechanisms: Degradation and beyond

Ford, P. W., Narasimhan, M., & Bennett, E. J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115050 · Cited by 22

Potato E3 ubiquitin ligase PUB27 negatively regulates drought tolerance by mediating stomatal movement

Tang, X., Ghimire, S., Liu, W., Fu, X., Zhang, H., Zhang, N., & Si, H. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.07.026 · Cited by 22

Regulation of ubiquitin and ubiquitin‐like modifiers by phosphorylation

Hepowit, N. L., Kolbe, C., Zelle, S. R., Latz, E., & MacGurn, J. A. (2021) · FEBS Journal · doi:10.1111/febs.16101 · Cited by 23

In silico APC/C substrate discovery reveals cell cycle-dependent degradation of UHRF1 and other chromatin regulators

Franks, J. L., Martinez‐Chacin, R. C., Wang, X., Tiedemann, R. L., Bonacci, T., Choudhury, R., Bolhuis, D. L., Enrico, T. P., Mouery, R. D., Damrauer, J. S., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000975 · Cited by 22

Branched ubiquitin code: from basic biology to targeted protein degradation

Ohtake, F. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac002 · Cited by 22

Acetylated Ubiquitin Modulates the Catalytic Activity of the E1 Enzyme Uba1

Lacoursiere, R. E., & Shaw, G. S. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00145 · Cited by 21

Poxvirus Interactions with the Host Ubiquitin System

Lant, S., & de Motes, C. M. (2021) · Pathogens · doi:10.3390/pathogens10081034 · Cited by 21

Interplay between ubiquitylation and SUMOylation: Empowered by phase separation

Jin, J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.h119.011037 · Cited by 21

Regulation of the conserved 3′ ‐ 5′ exoribonuclease EXOSC10 / Rrp6 during cell division, development and cancer

Stuparević, I., Novačić, A., Rahmouni, A. R., Fernandez, A., Lamb, N. J. C., & Primig, M. (2021) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12693 · Cited by 23

Ubiquitin-related processes and innate immunity in C. elegans

Garcia-Sanchez, J. A., Ewbank, J. J., & Visvikis, O. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03787-w · Cited by 21

Ubiquitin system mutations in neurological diseases

Zenge, C., & Ordureau, A. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.06.011 · Cited by 20

Targeted protein degradation: expanding the technology to facilitate the clearance of neurotoxic proteins in neurodegenerative diseases

Wang, X., Shuai, W., Yang, P., Liu, Y., Zhang, Y., & Wang, G. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102584 · Cited by 19

Development of Human Carbonic Anhydrase II Heterobifunctional Degraders

O’Herin, C., Moriuchi, Y. W., Bemis, T. A., Kohlbrand, A. J., Burkart, M. D., & Cohen, S. M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01843 · Cited by 23

Induced proximity to PML protects TDP-43 from aggregation via SUMO–ubiquitin networks

Wagner, K., Keiten‐Schmitz, J., Adhikari, B., Patra, U., Husnjak, K., McNicoll, F., Dormann, D., Müller-McNicoll, M., Tascher, G., Wolf, E., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01886-4 · Cited by 17

Inhibition of USP9X Downregulates JAK2-V617F and Induces Apoptosis Synergistically with BH3 Mimetics Preferentially in Ruxolitinib-Persistent JAK2-V617F-Positive Leukemic Cells

Akiyama, H., Umezawa, Y., Watanabe, D., Okada, K., Ishida, S., Nogami, A., & Miura, O. (2020) · Cancers · doi:10.3390/cancers12020406 · Cited by 17

SYVN1-mediated ubiquitylation directs localization of MCT4 in the plasma membrane to promote the progression of lung adenocarcinoma

Zhao, M., Huang, C., Yang, L., Pan, B., Yang, S., Chang, J., Yu, J. H., Zhao, G., Yue, D., Qie, S., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06208-x · Cited by 17

MVsim is a toolset for quantifying and designing multivalent interactions

Bruncsics, B., Errington, W. J., & Sarkar, C. A. (2022) · Nature Communications · doi:10.1038/s41467-022-32496-6 · Cited by 16

How Phosphorylation by PINK1 Remodels the Ubiquitin System: A Perspective from Structure and Dynamics

Tang, C., & Zhang, W. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00715 · Cited by 15

Post-translational modifications and stress adaptation: the paradigm of FKBP51

Rein, T. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190332 · Cited by 15

N-glycosylation and ubiquitinylation of PD-L1 do not restrict interaction with BMS-202: A molecular modeling study

Bailly, C., & Vergoten, G. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107362 · Cited by 16

Zebrafish Nedd8 facilitates ovarian development and the maintenance of female secondary sexual characteristics via suppression of androgen receptor activity

Yu, G., Liu, X., Zhang, D., Wang, J., Ouyang, G., Chen, Z., & Xiao, W. (2020) · Development · doi:10.1242/dev.194886 · Cited by 16

Erasing marks: Functions of plant deubiquitylating enzymes in modulating the ubiquitin code

Vogel, K., & Isono, E. (2024) · The Plant Cell · doi:10.1093/plcell/koae129 · Cited by 15

Arabidopsis CIRP1 E3 ligase modulates drought and oxidative stress tolerance and reactive oxygen species homeostasis by directly degrading catalases

Yang, H., Zhang, Y., Lyu, S., Mao, Y., Yu, F., Liu, S., Fang, Y., & Deng, S. (2025) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13845 · Cited by 15

Roles of Post-Translational Modifications of Transcription Factors Involved in Breast Cancer Hypoxia

Seymour, L., Nuru, N., Johnson, K. R., Villalpando-Gutierrez, J. M., Njoku, V. T., Darie, C. C., & Neagu, A.-N. (2025) · Molecules · doi:10.3390/molecules30030645 · Cited by 15

How Is the Fidelity of Proteins Ensured in Terms of Both Quality and Quantity at the Endoplasmic Reticulum? Mechanistic Insights into E3 Ubiquitin Ligases

Kang, J. A., & Jeon, Y. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042078 · Cited by 15

Screening of a Focused Ubiquitin-Proteasome Pathway Inhibitor Library Identifies Small Molecules as Novel Modulators of Botulinum Neurotoxin Type A Toxicity

Sen, E., Kota, K. P., Panchal, R. G., Bavari, S., & Kiris, E. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.763950 · Cited by 15

Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and Implicates UBE2D3 in Protein Quality Control

Yalçin, Z., Koot, D., Bezstarosti, K., Salas‐Lloret, D., Bleijerveld, O. B., Boersma, V., Falcone, M., González‐Prieto, R., Altelaar, M. A. F., Demmers, J., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100548 · Cited by 18

Histone ubiquitination: Role in genome integrity and chromatin organization

Ghate, N. B., Nadkarni, K. S., Barik, G. K., Tat, S. S., Sahay, O., & Santra, M. K. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195044 · Cited by 15

Advances on Plant Ubiquitylome—From Mechanism to Application

He, D., Damaris, R. N., Li, M., Khan, I., & Yang, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217909 · Cited by 17

Role of ubiquitination in arsenic tolerance in plants

Zhang, J., Wysocki, R., Li, F., Yu, M., Martinoia, E., & Song, W. (2023) · Trends in Plant Science · doi:10.1016/j.tplants.2023.03.008 · Cited by 15

Targeting a key disulfide linkage to regulate RIG-I condensation and cytosolic RNA-sensing

Wang, B., Wang, Y., Pan, T. S., Zhou, L., Ran, Y., Zou, J., Yan, X., Wen, Z., Lin, S., Ren, A., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01646-5 · Cited by 14

Recent advances in targeting protein degradation for tumor immunotherapy

Li, S., Jin, Y., Wu, H., Yuan, H., & Zhao, J. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01765-4 · Cited by 14

Ubiquitination of glycogen and metabolites in cells and tissues

Jochem, M., Cobbold, S. A., Goodman, C. A., Kueng, C., Cerra, A., Fielden, L. F., Kim, M. L., Schenk, P., Agarwal, R., Wang, X. S., et al. (2026) · Nature · doi:10.1038/s41586-026-10548-x · Cited by 14

Obesity of G2e3 Knockout Mice Suggests That Obesity-Associated Variants Near Human G2E3 Decrease G2E3 Activity

Powell, D. R., Doree, D. D., DaCosta, C. M., Platt, K. A., Hansen, G. M., Sligtenhorst, I. V., Ding, Z., Revelli, J., & Brommage, R. (2020) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s259546 · Cited by 14

Manipulating autophagic degradation in human diseases: from mechanisms to interventions

Zhang, Y., Liu, X., Klionsky, D. J., Lu, B., & Zhong, Q. (2022) · Life Medicine · doi:10.1093/lifemedi/lnac043 · Cited by 14

N-terminal acetylation can stabilize proteins independent of their ubiquitination

van de Kooij, B., de Vries, E., Rooswinkel, R. W., Janssen, G. M. C., Kok, F. K., van Veelen, P. A., & Borst, J. G. (2023) · Scientific Reports · doi:10.1038/s41598-023-32380-3 · Cited by 14

Histone modification in psoriasis: Molecular mechanisms and potential therapeutic targets

Liu, R., Zhang, L., & Zhang, K. (2024) · Experimental Dermatology · doi:10.1111/exd.15151 · Cited by 14

Synthesis of Branched Triubiquitin Active-Site Directed Probes

Liu, J., Li, Y., Deol, K. K., & Strieter, E. R. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b02406 · Cited by 15

Control of craniofacial and brain development by Cullin3-RING ubiquitin ligases: Lessons from human disease genetics

Asmar, A. J., Beck, D. B., & Werner, A. A. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112300 · Cited by 13

A Potential Mechanism for Targeting Aggregates With Proteasomes and Disaggregases in Liquid Droplets

Hayes, E. M., Sirvio, L., & Ye, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.854380 · Cited by 13

Oxidative versus Reductive Stress in Breast Cancer Development and Cellular Mechanism of Alleviation: A Current Perspective with Anti-breast Cancer Drug Resistance

Ray, S. K., Erukkambattu, J., Kotnis, A. L., & Mukherjee, S. (2023) · Current Molecular Medicine · doi:10.2174/1566524023666230309112751 · Cited by 14

N6-methyladenosine-modified MIB1 promotes stemness properties and peritoneal metastasis of gastric cancer cells by ubiquitinating DDX3X

Xu, P., Liu, K., Huang, S., Lv, J., Yan, Z., Ge, H., Cheng, Q., Chen, Z., Ji, P., Qian, Y., et al. (2024) · Gastric Cancer · doi:10.1007/s10120-023-01463-5 · Cited by 14

Autoimmunity and Autoinflammation: Relapsing Polychondritis and VEXAS Syndrome Challenge

Cardoneanu, A., Rezus, I. I., Burlui, A., Richter, P., Bratoiu, I., Mihai, I. R., Macovei, L. A., & Rezuş, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042261 · Cited by 13

E2–Ub-R74G strategy reveals E2-specific ubiquitin conjugation profiles in live cells

Shen, S., & Yin, H. H. (2025) · Nature Chemical Biology · doi:10.1038/s41589-024-01809-9 · Cited by 13

Protein quality control of N-methyl-D-aspartate receptors

Benske, T. M., Mu, T., & Wang, Y. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.907560 · Cited by 12

Hypertrophic cardiomyopathy in MYBPC3 carriers in aging

Ananthamohan, K., Stelzer, J. E., & Sadayappan, S. (2024) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2023.29 · Cited by 13

Wnt signalosomes: What we know that we do not know

Hartmann, H. A., Siddiqui, G. S., Bryant, J. M., Robbins, D. J., Weiss, V. L., Ahmed, Y. F., & Lee, E. N. (2024) · BioEssays · doi:10.1002/bies.202400110 · Cited by 12

The heat shock transcription factors regulate response mechanisms to abiotic stresses in plants

Wang, Y.-X., & Xu, J. (2025) · Crop Design · doi:10.1016/j.cropd.2025.100109 · Cited by 12

Boosting CAR T-cell efficacy by blocking proteasomal degradation of membrane antigens

Rieger, L., Irlinger, K., Füchsl, F., Tietje, M. R., Purcarea, A., Barbian, N., Faber, M., Vogelsang, C., Pfeuffer, L., Stotz, S., et al. (2025) · Blood · doi:10.1182/blood.2024027616 · Cited by 16

Dual-color pulse-chase ubiquitination assays to simultaneously monitor substrate priming and extension

Scott, D. C., & Schulman, B. A. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.01.004 · Cited by 12

Integrin-Driven Axon Regeneration in the Spinal Cord Activates a Distinctive CNS Regeneration Program

Cheah, M., Cheng, Y., Petrova, V., Cimpean, A., Jendelová, P., Swarup, V., Woolf, C. J., Geschwind, D. H., & Fawcett, J. W. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.2076-22.2023 · Cited by 13

Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase

Purser, N., Tripathi‐Giesgen, I., Li, J., Scott, D. C., Horn‐Ghetko, D., Baek, K., Schulman, B. A., Alpi, A. F., & Kleiger, G. (2023) · Biochemical Journal · doi:10.1042/bcj20230373 · Cited by 13

Strategy for Development of Site-Specific Ubiquitin Antibodies

van Kruijsbergen, I., Mulder, M. P. C., Uckelmann, M., van Welsem, T., de Widt, J., Spanjaard, A., Jacobs, H., Oualid, F. E., Ovaa, H., & van Leeuwen, F. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00111 · Cited by 12

The Mechanism of Ubiquitination or Deubiquitination Modifications in Regulating Solid Tumor Radiosensitivity

Zhang, M., Shao, Y., & Gu, W. (2023) · Biomedicines · doi:10.3390/biomedicines11123240 · Cited by 11

An RNF12-USP26 amplification loop drives germ cell specification and is disrupted by disease-associated mutations

Segarra-Fas, A., Espejo-Serrano, C., Bustos, F., Zhou, H., Wang, F., Toth, R. L., Macartney, T., Bach, I., Nardocci, G., & Findlay, G. M. (2022) · Science Signaling · doi:10.1126/scisignal.abm5995 · Cited by 11

E3 Ubiquitin Ligases: Structures, Biological Functions, Diseases, and Therapy

Wang, H., Peng, J., Li, H., Lan, Y., Guo, J., Qiu, Q., & Huang, X. (2025) · MedComm · doi:10.1002/mco2.70528 · Cited by 13

Uncovering new insights into the role of the ubiquitin ligase Smurf1 on the regulation of innate immune signaling and resistance to infection

Souza‐Costa, L. P., Andrade-Chaves, J. T., Andrade, J. M., Costa, V. V., & Franco, L. H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1185741 · Cited by 10

Inhibition of the Ubiquitin Transfer Cascade by a Peptidomimetic Foldamer Mimicking the E2 N-Terminal Helix

Zhou, L., Jeong, I. H., Xue, S., Xue, M., Wang, L., Li, S., Liu, R., Jeong, G. H., Wang, X., Cai, J., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01459 · Cited by 10

Cellular Functions of Deubiquitinating Enzymes in Ovarian Adenocarcinoma

Min, Y., Park, H., Baek, K., & Hwang, S. (2023) · Genes · doi:10.3390/genes14040886 · Cited by 10

A General in Vitro Assay for Studying Enzymatic Activities of the Ubiquitin System

Zuo, Y., Chong, B. K., Jiang, K., Finley, D. J., Klenerman, D., & Ye, Y. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b00602 · Cited by 10

Analysis of 26S Proteasome Activity across Arabidopsis Tissues

Ganapathy, J., Hand, K. A., & Shabek, N. (2024) · Plants · doi:10.3390/plants13121696 · Cited by 9

UCHL5 is a putative prognostic marker in renal cell carcinoma: a study of UCHL family

Zhang, M., Li, J., Liu, S., Zhou, F., & Zhang, L. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00192-0 · Cited by 9

The Ubiquitin Tale: Current Strategies and Future Challenges

Upadhyay, A., & Joshi, V. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00278 · Cited by 11

Recent Advances in Ubiquitin Signals Regulating Plant Membrane Trafficking

Hasegawa, Y., Luo, Y., & Sato, T. (2024) · Plant and Cell Physiology · doi:10.1093/pcp/pcae123 · Cited by 9

Time as a danger signal promoting G1 arrest after mitosis

Fulcher, L. J., Batley, C., Sobajima, T., & Barr, F. A. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.06.001 · Cited by 9

Interplay between ubiquitination and ADP-ribosylation and the case of dual modification ADPr-Ub

Zhu, K., Chatrin, C., Smith, R., Ahel, D., & Ahel, I. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253040 · Cited by 9

Deubiquitinating enzymes UBP12 and UBP13 regulate carbon/nitrogen-nutrient stress responses by interacting with the membrane-localized ubiquitin ligase ATL31 in Arabidopsis

Luo, Y., Yasuda, S., Takagi, J., Hasegawa, Y., Chiba, Y., Yamaguchi, J., & Sato, T. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.10.089 · Cited by 9

A cell-permeable Ub-Dha probe for profiling E1–E2–E3 enzymes in live cells

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