Protein neddylation and its role in health and diseases
Open accessAbstract
NEDD8 (Neural precursor cell expressed developmentally downregulated protein 8) is an ubiquitin-like protein that is covalently attached to a lysine residue of a protein substrate through a process known as neddylation, catalyzed by the enzyme cascade, namely NEDD8 activating enzyme (E1), NEDD8 conjugating enzyme (E2), and NEDD8 ligase (E3). The substrates of neddylation are categorized into cullins and non-cullin proteins. Neddylation of cullins activates CRLs (cullin RING ligases), the largest family of E3 ligases, whereas neddylation of non-cullin substrates alters their stability and activity, as well as subcellular localization. Significantly, the neddylation pathway and/or many neddylation substrates are abnormally activated or over-expressed in various human diseases, such as metabolic disorders, liver dysfunction, neurodegenerative disorders, and cancers, among others. Thus, targeting neddylation becomes an attractive strategy for the treatment of these diseases. In this review, we first provide a general introduction on the neddylation cascade, its biochemical process and regulation, and the crystal structures of neddylation enzymes in complex with cullin substrates; then discuss how neddylation governs various key biological processes via the modification of cullins and non-cullin substrates. We further review the literature data on dysregulated neddylation in several human diseases, particularly cancer, followed by an outline of current efforts in the discovery of small molecule inhibitors of neddylation as a promising therapeutic approach. Finally, few perspectives were proposed for extensive future investigations.
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DCUN1D5 is involved in the neddylation pathway that regulates protein homeostasis.
“DCUN1D5 is involved in the neddylation pathway that regulates protein homeostasis, 58 and S100A12 is a pro‐inflammatory mediator that modulates neuroinflammation. 59”
From Unraveling sex differences in Alzheimer's disease and related endophenotypes with brain proteomes (2025) · cites this paper as [58]
DCUN1D5 regulates the protein neddylation pathway that has been linked to AD.
“Moreover, TRIM46 and TOGARAM1 are proteins that play roles in microtubule functions, 55 , 56 and DCUN1D5 regulates the protein neddylation pathway that has been linked to AD. 58”
From Unraveling sex differences in Alzheimer's disease and related endophenotypes with brain proteomes (2025) · cites this paper as [58]
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Dendritic cells and the control of immunity
Banchereau, J., & Steinman, R. M. (1998) · Nature · doi:10.1038/32588 · Cited by 14,244 · see citing works
Control of Regulatory T Cell Development by the Transcription Factor <i>Foxp3</i>
Hori, S., Nomura, T., & Sakaguchi, S. (2003) · Science · doi:10.1126/science.1079490 · Cited by 8,187 · see citing works
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works
Comprehensive molecular characterization of gastric adenocarcinoma
The Cancer Genome Atlas Research Network (2014) · Nature · doi:10.1038/nature13480 · Cited by 6,498 · see citing works
Self-citationHeart Disease and Stroke Statistics—2022 Update: A Report From the American Heart Association
Tsao, C. W., Aday, A. W., Almarzooq, Z. I., Alonso, A., Beaton, A. Z., Bittencourt, M. S., Boehme, A. K., Buxton, A. E., Carson, A. P., Commodore-Mensah, Y., et al. (2022) · Circulation · doi:10.1161/cir.0000000000001052 · Cited by 5,987 · see citing works
Integrated genomic characterization of endometrial carcinoma
The Cancer Genome Atlas Research Network, & Levine, D. A. (2013) · Nature · doi:10.1038/nature12113 · Cited by 5,784 · see citing works
Neutrophil recruitment and function in health and inflammation
Kolaczkowska, E., & Kubes, P. (2013) · Nature Reviews Immunology · doi:10.1038/nri3399 · Cited by 5,472 · see citing works
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630 · see citing works
Functional Expression Cloning of Nanog, a Pluripotency Sustaining Factor in Embryonic Stem Cells
Chambers, I., Colby, D., Robertson, M., Nichols, J., Lee, S., Tweedie, S., & Smith, A. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00392-1 · Cited by 3,255 · see citing works
Inflammation and tumor progression: signaling pathways and targeted intervention
Zhao, H., Wu, L., Yan, G., Chen, Y., Zhou, M., Wu, Y., & Li, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00658-5 · Cited by 2,907 · see citing works
Non-alcoholic fatty liver disease
Powell, E. E., Wong, V. W.-S., & Rinella, M. (2021) · The Lancet · doi:10.1016/s0140-6736(20)32511-3 · Cited by 2,789 · 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
T cell exclusion, immune privilege, and the tumor microenvironment
Joyce, J. A., & Fearon, D. T. (2015) · Science · doi:10.1126/science.aaa6204 · Cited by 2,494 · see citing works
Zou, W., Wolchok, J. D., & Chen, L. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad7118 · Cited by 2,382 · see citing works
Cellular senescence in ageing: from mechanisms to therapeutic opportunities
Di Micco, R., Krizhanovsky, V., Baker, D., & d’Adda di Fagagna, F. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00314-w · Cited by 2,277 · see citing works
Necroptosis, pyroptosis and apoptosis: an intricate game of cell death
Bertheloot, D., Latz, E., & Franklin, B. S. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00630-3 · Cited by 2,198 · see citing works
Smith-Garvin, J. E., Koretzky, G. A., & Jordan, M. S. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132706 · Cited by 2,144 · see citing works
From Krebs to clinic: glutamine metabolism to cancer therapy
Altman, B. J., Stine, Z. E., & Dang, C. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.71 · Cited by 2,119 · see citing works
Inflammation in obesity, diabetes, and related disorders
Rohm, T. V., Meier, D. T., Olefsky, J. M., & Donath, M. Y. (2022) · Immunity · doi:10.1016/j.immuni.2021.12.013 · Cited by 2,066 · see citing works
Tumor angiogenesis: causes, consequences, challenges and opportunities
Lugano, R., Ramachandran, M., & Dimberg, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03351-7 · Cited by 2,040 · see citing works
An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
Soucy, T. A., Smith, P. G., Milhollen, M. A., Berger, A. J., Gavin, J. M., Adhikari, S., Brownell, J. E., Burke, K. E., Cardin, D. P., Critchley, S., et al. (2009) · Nature · doi:10.1038/nature07884 · Cited by 1,990 · see citing works
ATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response
Blackford, A. N., & Jackson, S. P. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.015 · Cited by 1,953 · see citing works
The non-canonical NF-κB pathway in immunity and inflammation
Sun, S. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.52 · Cited by 1,911 · see citing works
Analysis of lung tumor initiation and progression using conditional expression of oncogenic K-rasPreprint
Jackson, E. L., Willis, N. A., Mercer, K. L., Bronson, R. T., Crowley, D. G., Montoya, R., Jacks, T., & Tuveson, D. A. (2001) · Genes & Development · doi:10.1101/gad.943001 · Cited by 1,877 · see citing works
Histone deacetylases and cancer: causes and therapies
Marks, P. A., Rifkind, R. A., Richon, V. M., Breslow, R., Miller, T., & Kelly, W. K. (2001) · Nature reviews. Cancer · doi:10.1038/35106079 · Cited by 1,866 · see citing works
Artificial intelligence in drug discovery and development
Paul, D., Sanap, G., Shenoy, S., Kalyane, D., Kalia, K., & Tekade, R. K. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.010 · Cited by 1,695 · see citing works
The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway
Baird, L., & Yamamoto, M. P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-20 · Cited by 1,600 · see citing works
Ohh, M., Park, C. W., Ivan, M., Hoffman, M. A., Kim, T.-Y., Huang, L. E., Pavletich, N., Chau, V., & Kaelin, W. G. (2000) · Nature Cell Biology · doi:10.1038/35017054 · Cited by 1,577 · see citing works
Matthews, H. K., Bertoli, C., & de Bruin, R. A. M. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00404-3 · Cited by 1,506 · see citing works
Anti–PD-1/PD-L1 therapy of human cancer: past, present, and future
Chen, L., & Han, X. N. (2015) · Journal of Clinical Investigation · doi:10.1172/jci80011 · Cited by 1,433 · see citing works
Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425 · see citing works
NF-κB in the liver—linking injury, fibrosis and hepatocellular carcinoma
Luedde, T., & Schwabe, R. F. (2011) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.213 · Cited by 1,345 · see citing works
Role of RNA modifications in cancer
Barbieri, I., & Kouzarides, T. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0253-2 · Cited by 1,322 · see citing works
Mitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306 · see citing works
Atherosclerosis: Recent developments
Björkegren, J., & Lusis, A. J. (2022) · Cell · doi:10.1016/j.cell.2022.04.004 · Cited by 1,301 · see citing works
Michael, M. D., Kulkarni, R. N., Postic, C., Previs, S. F., Shulman, G. I., Magnuson, M. A., & Kahn, C. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00015-8 · Cited by 1,296 · see citing works
Mitochondrial metabolism and cancer
Porporato, P. E., Filigheddu, N., Pedro, J. M. B., Kroemer, G., & Galluzzi, L. (2017) · Cell Research · doi:10.1038/cr.2017.155 · Cited by 1,292 · see citing works
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works
Peterson, T. R., Laplante, M., Thoreen, C. C., Sancak, Y., Kang, S. A., Kuehl, W. M., Gray, N. S., & Sabatini, D. M. (2009) · Cell · doi:10.1016/j.cell.2009.03.046 · Cited by 1,202 · see citing works
A comprehensive pathway map of epidermal growth factor receptor signaling
Oda, K., Matsuoka, Y., Funahashi, A., & Kitano, H. (2005) · Molecular Systems Biology · doi:10.1038/msb4100014 · Cited by 1,163 · see citing works
Targeting HER2-positive breast cancer: advances and future directions
Swain, S. M., Shastry, M., & Hamilton, E. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00579-0 · Cited by 1,160 · see citing works
Simsek, T., Kocabas, F., Zheng, J., DeBerardinis, R. J., Mahmoud, A. I., Olson, E. N., Schneider, J. W., Zhang, C. C., & Sadek, H. A. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.07.011 · Cited by 1,101 · see citing works
Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity
Li, C., Lim, S., Xia, W., Lee, H., Chan, L.-C., Kuo, C., Khoo, K., Chang, S.-S., Cha, J., Kim, T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12632 · Cited by 1,100 · see citing works
Hori, S., Nomura, T., & Sakaguchi, S. (2017) · The Journal of Immunology · doi:10.1093/jimmunol/198.3.981 · Cited by 1,067 · see citing works
Reactive Oxygen Species in Cancer: Current Findings and Future Directions
Nakamura, H., & Takada, K. (2021) · Cancer Science · doi:10.1111/cas.15068 · Cited by 1,027 · see citing works
Cyclin D–CDK4 kinase destabilizes PD-L1 via cullin 3–SPOP to control cancer immune surveillance
Zhang, J., Bu, X., Wang, H., Zhu, Y., Geng, Y., Nihira, N. T., Tan, Y., Ci, Y., Wu, F., Dai, X., et al. (2018) · Nature · doi:10.1038/nature25015 · Cited by 1,013 · see citing works
Self-citationOxygen Sensing, Homeostasis, and Disease
Semenza, G. L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1011165 · Cited by 989 · see citing works
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Re, D. P. D., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 979 · see citing works
PPAR control of metabolism and cardiovascular functions
Montaigne, D., Butruille, L., & Staels, B. (2021) · Nature Reviews Cardiology · doi:10.1038/s41569-021-00569-6 · Cited by 960 · see citing works
King, R. W., Peters, J., Tugendreich, S., Rolfe, M., Hieter, P., & Kirschner, M. W. (1995) · Cell · doi:10.1016/0092-8674(95)90338-0 · Cited by 956 · see citing works
TGFβ biology in cancer progression and immunotherapy
Derynck, R., Turley, S. J., & Akhurst, R. J. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0403-1 · Cited by 944 · see citing works
Marino, S., Vooijs, M., van der Gulden, H., Jonkers, J., & Berns, A. (2000) · Genes & Development · doi:10.1101/gad.14.8.994 · Cited by 920 · see citing works
Regulation of the HIF-1α Level Is Essential for Hematopoietic Stem Cells
Takubo, K., Goda, N., Yamada, W., Iriuchishima, H., Ikeda, E., Kubota, Y., Shima, H., Johnson, R. S., Hirao, A., Suematsu, M., et al. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.06.020 · Cited by 891 · see citing works
Targeting DNA damage response pathways in cancer
Groelly, F. J., Fawkes, M., Dagg, R. A., Blackford, A. N., & Tarsounas, M. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00535-5 · Cited by 868 · see citing works
Immunoregulatory functions of mTOR inhibition
Thomson, A. W., Turnquist, H. R., & Raimondi, G. (2009) · Nature reviews. Immunology · doi:10.1038/nri2546 · Cited by 849 · see citing works
REST and Its Corepressors Mediate Plasticity of Neuronal Gene Chromatin throughout Neurogenesis
Ballas, N., Grunseich, C., Lu, D. D., Speh, J. C., & Mandel, G. (2005) · Cell · doi:10.1016/j.cell.2005.03.013 · Cited by 846 · see citing works
Control of protein stability by post-translational modifications
Lee, J. M., Hammarén, H. M., Savitski, M. M., & Baek, S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-35795-8 · Cited by 822 · 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
Hepatic inflammatory responses in liver fibrosis
Hammerich, L., & Tacke, F. (2023) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-023-00807-x · Cited by 803 · see citing works
Groszer, M., Erickson, R., Scripture-Adams, D. D., Lesche, R., Trumpp, A., Zack, J. A., Kornblum, H. I., Liu, X., & Wu, H. (2001) · Science · doi:10.1126/science.1065518 · Cited by 798 · see citing works
Hinz, M., Krappmann, D., Eichten, A., Heder, A., Scheidereit, C., & Strauss, M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2690 · Cited by 788 · see citing works
Post-translational modifications in proteins: resources, tools and prediction methods
Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 787 · see citing works
Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767 · see citing works
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 757 · see citing works
Metabolomics and Metabolic Diseases: Where Do We Stand?
Newgard, C. B. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.018 · Cited by 756 · see citing works
Mechanistic Pathways of Sex Differences in Cardiovascular Disease
Regitz‐Zagrosek, V., & Kararigas, G. (2016) · Physiological Reviews · doi:10.1152/physrev.00021.2015 · Cited by 738 · see citing works
Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome
Lyapina, S., Cope, G. A., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D. A., Wei, N., Shevchenko, A., & Deshaies, R. J. (2001) · Science · doi:10.1126/science.1059780 · Cited by 699 · see citing works
Epigenetics in health and disease
Zhang, L., Lu, Q., & Chang, C. (2020) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-15-3449-2_1 · Cited by 689 · see citing works
Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1
Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075901 · Cited by 682 · see citing works
O’Neil, J., Grim, J. A., Strack, P. R., Rao, S. S., Tibbitts, D., Winter, C. G., Hardwick, J. S., Welcker, M., Meijerink, J. P. P., Pieters, R., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070876 · Cited by 662 · 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
The Role of Hypoxia in Development of the Mammalian Embryo
Dunwoodie, S. L. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.11.008 · Cited by 651 · see citing works
Liquid–liquid phase separation in human health and diseases
Wang, B., Zhang, L., Dai, T., Qin, Z.-R., Lu, H.-S., Zhang, L., & Zhou, F.-F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00678-1 · Cited by 634 · see citing works
Protein neddylation: beyond cullin–RING ligases
Enchev, R. I., Schulman, B. A., & Peter, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3919 · Cited by 622 · see citing works
Structure of a β-TrCP1-Skp1-β-Catenin Complex
Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612 · see citing works
Signaling to p53: ribosomal proteins find their way
Zhang, Y., & Lu, H. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.024 · Cited by 591 · see citing works
Animal models of neurodegenerative diseases
Dawson, T. M., Golde, T. E., & Lagier-Tourenne, C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0236-8 · Cited by 576 · see citing works
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 · see citing works
Identification of a set of genes with developmentally down-regulated expression in the mouse brain
Kumar, S., Tomooka, Y., & Noda, M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91747-e · Cited by 552 · see citing works
Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism
Cappadocia, L., & Lima, C. D. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00737 · Cited by 548 · see citing works
NF-κB: blending metabolism, immunity, and inflammation
Capece, D., Verzella, D., Flati, I., Arboretto, P., Cornice, J., & Franzoso, G. (2022) · Trends in Immunology · doi:10.1016/j.it.2022.07.004 · Cited by 538 · see citing works
Characterization of NEDD8, a Developmentally Down-regulated Ubiquitin-like Protein
Kamitani, T., Kito, K., Nguyen, H. P., & Yeh, E. T. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28557 · Cited by 535 · see citing works
Kettenbach, A. N., Schweppe, D. K., Faherty, B. K., Pechenick, D. A., Pletnev, A. A., & Gerber, S. A. (2011) · Science Signaling · doi:10.1126/scisignal.2001497 · Cited by 531 · see citing works
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521 · see citing works
The effect of HIF on metabolism and immunity
Taylor, C. T., & Scholz, C. C. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00587-8 · Cited by 517 · see citing works
ROS production by mitochondria: function or dysfunction?
Palma, F. R., Gantner, B. N., Sakiyama, M. J., Filho, C. K. C., Shukla, S., Lacchini, R., Cunniff, B., & Bonini, M. G. (2023) · Oncogene · doi:10.1038/s41388-023-02907-z · Cited by 516 · see citing works
Deactivation of Hepatic Stellate Cells During Liver Fibrosis Resolution in Mice
Troeger, J. S., Mederacke, I., Gwak, G., Dapito, D. H., Mu, X., Hsu, C. C., Pradere, J., Friedman, R. A., & Schwabe, R. F. (2012) · Gastroenterology · doi:10.1053/j.gastro.2012.06.036 · Cited by 515 · see citing works
PKM2, cancer metabolism, and the road ahead
Dayton, T. L., Jacks, T., & Vander Heiden, M. G. (2016) · The EMBO Reports · doi:10.15252/embr.201643300 · Cited by 515 · see citing works
Leptin- and Leptin Receptor-Deficient Rodent Models: Relevance for Human Type 2 Diabetes
Wang, B., Chandrasekera, P. C., & Pippin, J. J. (2014) · Current Diabetes Reviews · doi:10.2174/1573399810666140508121012 · Cited by 511 · see citing works
Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works
Mouse models of inflammatory bowel disease☆
Wirtz, S. J., & Neurath, M. F. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.07.003 · Cited by 508 · see citing works
Epigenetic regulation in metabolic diseases: mechanisms and advances in clinical study
Wu, Y., Lin, Z., Li, C., Lin, X. J., Shan, S., Guo, B., Zheng, M.-H., Li, F., Yuan, L., & Li, Z. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01333-7 · Cited by 507 · see citing works
Self-citationZhou, H., Zhang, J., Zhang, X., & Li, Q. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00430-1 · Cited by 485 · see citing works
The SCFFBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia
Thompson, B. J., Buonamici, S., Sulis, M. L., Palomero, T., Vilimas, T., Basso, G., Ferrando, A. A., & Aifantis, I. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070872 · Cited by 479 · see citing works
M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCF <sup>β-TrCP</sup>
Watanabe, N., Arai, H., Nishihara, Y., Taniguchi, M., Watanabe, N., Hunter, T., & Osada, H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307700101 · Cited by 472 · see citing works
Biddinger, S. B., Hernandez-Ono, A., Rask-Madsen, C., Haas, J. T., Alemán, J. O., Suzuki, R., Scapa, E. F., Agarwal, C., Carey, M. C., Stephanopoulos, G., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.013 · Cited by 469 · see citing works
Brownell, J. E., Sintchak, M. D., Gavin, J. M., Liao, H., Bruzzese, F. J., Bump, N. J., Soucy, T. A., Milhollen, M. A., Yang, X., Burkhardt, A. L., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.024 · Cited by 468 · see citing works
Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W., & Pavletich, N. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.022 · Cited by 464 · see citing works
Ohta, T., Michel, J. J. C., Schottelius, A. J. G., & Xiong, Y. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80482-7 · Cited by 461 · see citing works
The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation
Fischer, E. S., Scrima, A., Böhm, K., Matsumoto, S., Lingaraju, G. M., Faty, M., Yasuda, T., Cavadini, S., Wakasugi, M., Hanaoka, F., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.035 · Cited by 460 · see citing works
Rigbolt, K. T. G., Prokhorova, T. A., Akimov, V., Henningsen, J., Johansen, P. T., Kratchmarova, I., Kassem, M., Mann, M., Olsen, J. V., & Blagoev, B. (2011) · Science Signaling · doi:10.1126/scisignal.2001570 · Cited by 451 · see citing works
Drugging the undruggables: exploring the ubiquitin system for drug development
Huang, X., & Dixit, V. M. (2016) · Cell Research · doi:10.1038/cr.2016.31 · Cited by 427 · cited 2× · see citing works
“465 Despite these challenges, several research teams have put the efforts to discover small molecule inhibitors for this seemingly “ undruggable ” target.”
BackgroundFBXW7 Targets mTOR for Degradation and Cooperates with PTEN in Tumor Suppression
Mao, J., Kim, I.-J., Wu, D., Climent, J., Kang, H. C., Delrosario, R., & Balmain, A. (2008) · Science · doi:10.1126/science.1162981 · Cited by 425 · see citing works
Higa, L. A., Wu, M., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1490 · Cited by 414 · see citing works
The COP9 signalosome: more than a protease
Wei, N., Serino, G., & Deng, X. L. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.09.004 · Cited by 413 · see citing works
Prodromal Parkinson disease subtypes — key to understanding heterogeneity
Berg, D., Borghammer, P., Fereshtehnejad, S.-M., Heinzel, S., Horsager, J., Schaeffer, E., & Postuma, R. B. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00486-9 · Cited by 409 · see citing works
Seol, J. H., Feldman, R. M. R., Zachariae, W., Shevchenko, A., Correll, C. C., Lyapina, S., Chi, Y., Gálová, M., Claypool, J. T., Sandmeyer, S. B., et al. (1999) · Genes & Development · doi:10.1101/gad.13.12.1614 · Cited by 403 · see citing works
Cao, W., Manicassamy, S., Tang, H., Kasturi, S. P., Pirani, A. M., Murthy, N., & Pulendran, B. (2008) · Nature Immunology · doi:10.1038/ni.1645 · Cited by 399 · see citing works
Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection
Otten, E. G., Werner, E., Crespillo-Casado, A., Boyle, K. B., Dharamdasani, V., Pathe, C., Santhanam, B., & Randow, F. (2021) · Nature · doi:10.1038/s41586-021-03566-4 · Cited by 395 · see citing works
Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation
Xiong, H., Wang, D., Chen, L., Choo, Y. S., Ma, H., Tang, C., Xia, K., Jiang, W. B., Ronai, Z. A., Zhuang, X., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37617 · Cited by 394 · see citing works
Two E3 ubiquitin ligases, SCF‐Skp2 and DDB1‐Cul4, target human Cdt1 for proteolysis
Nishitani, H., Sugimoto, N., Roukos, V., Nakanishi, Y., Saijo, M., Obuse, C., Tsurimoto, T., Nakayama, K., Nakayama, K., Fujita, M., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601002 · Cited by 392 · see citing works
Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics
Bennett, E. J., Rush, A. J., Gygi, S. P., & Harper, J. W. (2010) · Cell · doi:10.1016/j.cell.2010.11.017 · Cited by 386 · see citing works
The expression of adipogenic genes is decreased in obesity and diabetes mellitus
Nadler, S. T., Stoehr, J. P., Schueler, K. L., Tanimoto, G., Yandell, B. S., & Attie, A. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.21.11371 · Cited by 386 · see citing works
Bouchard, J. J., Otero, J. H., Scott, D. C., Szulc, E., Martin, E. W., Sabri, N., Granata, D., Marzahn, M. R., Lindorff‐Larsen, K., Salvatella, X., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.027 · Cited by 382 · see citing works
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Schmidt, M. F., Gan, Z. Y., Komander, D., & Dewson, G. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00706-7 · Cited by 373 · see citing works
van der Veen, A. G., & Ploegh, H. L. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-093010-153308 · Cited by 364 · see citing works
Nedd8 Modification of Cul-1 Activates SCF<sup>βTrCP</sup>-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 · see citing works
A novel protein modification pathway related to the ubiquitin system
Liakopoulos, D., Doenges, G., Matuschewski, K., & Jentsch, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.8.2208 · Cited by 361 · see citing works
Function and regulation of protein neddylation
Rabut, G. E. E., & Peter, M. (2008) · EMBO Reports · doi:10.1038/embor.2008.183 · Cited by 351 · see citing works
The Ubiquitin Ligase FBXW7 Modulates Leukemia-Initiating Cell Activity by Regulating MYC Stability
King, B., Trimarchi, T., Reavie, L. B., Xu, L., Mullenders, J., Ntziachristos, P., Aranda-Orgillés, B., Pérez-García, A., Shi, J., Vakoc, C. R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.041 · Cited by 347 · see citing works
Recruitment of a ROC1–CUL1 Ubiquitin Ligase by Skp1 and HOS to Catalyze the Ubiquitination of IκBα
Tan, P., Fuchs, S. Y., Chen, A., Wu, K. K.-Y., Gomez, C., Ronai, Z. A., & Pan, Z. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80481-5 · Cited by 345 · see citing works
Clinical Relevance of Microsatellite Instability in Colorectal Cancer
de la Chapelle, A., & Hampel, H. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.27.0652 · Cited by 333 · see citing works
The Role of Erk1 and Erk2 in Multiple Stages of T Cell Development
Fischer, A. M., Katayama, C. D., Pagès, G., Pouysségur, J., & Hedrick, S. Μ. (2005) · Immunity · doi:10.1016/j.immuni.2005.08.013 · Cited by 330 · see citing works
Building and remodelling Cullin–RING E3 ubiquitin ligases
Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327 · see citing works
Milhollen, M. A., Traore, T., Duffy, J., Thomas, M. P., Berger, A., Dang, L., Dick, L. R., Garnsey, J., Koenig, E. M., Langston, S., et al. (2010) · Blood · doi:10.1182/blood-2010-03-272567 · Cited by 324 · see citing works
BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2379 · Cited by 319 · see citing works
NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
Liu, J., Furukawa, M., Matsumoto, T., & Xiong, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00783-9 · Cited by 319 · see citing works
Ribosome biogenesis in disease: new players and therapeutic targets
Jiao, L., Liu, Y., Yu, X., Pan, X., Zhang, Y., Tu, J., Song, Y., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01285-4 · Cited by 317 · see citing works
Lammer, D., Mathias, N., Laplaza, J. M., Jiang, W., Liu, Y., Callis, J., Goebl, M. G., & Estelle, M. A. (1998) · Genes & Development · doi:10.1101/gad.12.7.914 · Cited by 312 · see citing works
Hepatitis B Virus X Protein Promotes Degradation of SMC5/6 to Enhance HBV Replication
Murphy, C. M., Xu, Y., Li, F., Nio, K., Reszka-Blanco, N., Li, X., Wu, Y., Yu, Y., Xiong, Y., & Su, L. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.026 · Cited by 312 · see citing works
CAND1 Binds to Unneddylated CUL1 and Regulates the Formation of SCF Ubiquitin E3 Ligase Complex
Zheng, J., Yang, X., Harrell, J. M., Ryzhikov, S., Shim, E., Lykke‐Hartmann, K., Wei, N., Sun, H., Kobayashi, R., & Zhang, H. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00784-0 · Cited by 309 · see citing works
Dimethyl fumarate in the treatment of relapsing–remitting multiple sclerosis: an overview
Bomprezzi, R. (2015) · Therapeutic Advances in Neurological Disorders · doi:10.1177/1756285614564152 · Cited by 301 · see citing works
The KEAP1-NRF2 pathway: Targets for therapy and role in cancer
Adinolfi, S., Patinen, T., Deen, A. J., Pitkänen, S., Härkönen, J., Kansanen, E., Küblbeck, J., & Levonen, A. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102726 · Cited by 301 · see citing works
Full-coverage regulations of autophagy by ROS: from induction to maturation
Zhou, J., Li, X., Liu, Y. J., Ji, F., Wu, Y., Shen, H., & Lu, G. (2021) · Autophagy · doi:10.1080/15548627.2021.1984656 · Cited by 300 · see citing works
Experimental animal models for rheumatoid arthritis
Choudhary, N., Bhatt, L. K., & Prabhavalkar, K. S. (2018) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2018.1434793 · Cited by 296 · see citing works
Lin, J. J., Milhollen, M. A., Smith, P. G., Narayanan, U., & Dutta, A. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2062 · Cited by 293 · see citing works
E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification
Huang, D. T. C., Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G. A. M., Murray, P. J., Roussel, M. F., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.011 · Cited by 282 · see citing works
Walden, H., Podgorski, M. S., Huang, D. T. C., Miller, D. W., Howard, R. J., Minor, D. L., Holton, J. M., & Schulman, B. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00452-0 · Cited by 282 · see citing works
Goldenberg, S. J., Cascio, T. C., Shumway, S. D., Garbutt, K. C., Liu, J., Xiong, Y., & Zheng, N. (2004) · Cell · doi:10.1016/j.cell.2004.10.019 · Cited by 280 · see citing works
Cullin-RING Ligases as Attractive Anti-cancer Targets
Zhao, Y., & Sun, Y. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990300 · Cited by 277 · see citing works
Self-citationSCFβ-TRCP controls oncogenic transformation and neural differentiation through REST degradation
Westbrook, T. F., Hu, G., Ang, X. L., Mulligan, P., Pavlova, N. N., Liang, A., Leng, Y., Maehr, R., Shi, Y., Harper, J. W., et al. (2008) · Nature · doi:10.1038/nature06780 · Cited by 275 · see citing works
Inhibition of NEDD8-activating enzyme: a novel approach for the treatment of acute myeloid leukemia
Swords, R. T., Kelly, K. R., Smith, P. G., Garnsey, J., Mahalingam, D., Medina, E. C., Oberheu, K., Padmanabhan, S., O'Dwyer, M. E., Nawrocki, S. T., et al. (2010) · Blood · doi:10.1182/blood-2009-11-254862 · Cited by 275 · see citing works
Identification of the Activating and Conjugating Enzymes of the NEDD8 Conjugation Pathway
Gong, L., & Yeh, E. T. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.12036 · Cited by 273 · see citing works
Zhao, Y., Xiong, X., & Sun, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.029 · Cited by 270 · see citing works
Self-citationChen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Ding, M., Peng, H. B., & Shao, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.004 · Cited by 270 · see citing works
Self-citationKamura, T., Conrad, M. N., Yan, Q., Conaway, R. C., & Conaway, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.22.2928 · Cited by 270 · see citing works
N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex
Scott, D. C., Monda, J. K., Bennett, E. J., Harper, J. W., & Schulman, B. A. (2011) · Science · doi:10.1126/science.1209307 · Cited by 270 · see citing works
NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly
Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020) · Nature · doi:10.1038/s41586-020-2000-y · Cited by 270 · see citing works
Regulation of Pluripotency and Cellular Reprogramming by the Ubiquitin-Proteasome System
Buckley, S. M., Aranda-Orgillés, B., Strikoudis, A., Apostolou, E., Loizou, E., Moran-Crusio, K., Farnsworth, C. L., Koller, A. A., DasGupta, R., Silva, J. C., et al. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.09.011 · Cited by 268 · see citing works
A new NEDD8-ligating system for cullin-4APreprint
Osaka, F., Kawasaki, H., Aida, N., Saeki, M., Chiba, T., Kawashima, S., Tanaka, K., & Kato, S. (1998) · Genes & Development · doi:10.1101/gad.12.15.2263 · Cited by 255 · see citing works
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome
Bian, Y., Song, C., Cheng, K., Dong, M., Wang, F., Huang, J., Sun, D., Wang, L., Ye, M., & Zou, H. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.11.014 · Cited by 253 · see citing works
Neddylation: a novel modulator of the tumor microenvironment
Zhou, L., Jiang, Y., Luo, Q. F., Li, L., & Jia, L. (2019) · Molecular Cancer · doi:10.1186/s12943-019-0979-1 · Cited by 252 · see citing works
mTOR Drives Its Own Activation via SCFβTrCP-Dependent Degradation of the mTOR Inhibitor DEPTOR
Gao, D., Inuzuka, H., Tan, M.-K. M., Fukushima, H., Locasale, J. W., Liu, P., Wan, L., Zhai, B., Chin, Y. R., Shaik, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.030 · Cited by 248 · see citing works
Cancer epigenetics in clinical practice
Dávalos, V., & Esteller, M. (2022) · CA A Cancer Journal for Clinicians · doi:10.3322/caac.21765 · Cited by 244 · see citing works
Targeting Neddylation Pathways to Inactivate Cullin-RING Ligases for Anticancer Therapy
Zhao, Y., Morgan, M. A., & Sun, Y. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5795 · Cited by 242 · see citing works
Self-citation(2012) · doi:10.1158/0008-5472.can-12-0388 · Cited by 242 · see citing works
Self-citationHistone 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
Swords, R. T., Erba, H. P., DeAngelo, D. J., Bixby, D. L., Altman, J. K., Maris, M. B., Hua, Z., Blakemore, S. J., Faessel, H. M., Sedarati, F., et al. (2015) · British Journal of Haematology · doi:10.1111/bjh.13323 · Cited by 232 · see citing works
Crystal structure of the human COP9 signalosome
Lingaraju, G. M., Bunker, R. D., Cavadini, S., Heß, D., Hassiepen, U., Renatus, M., Fischer, E. S., & Thomä, N. H. (2014) · Nature · doi:10.1038/nature13566 · Cited by 231 · see citing works
Jia, S., Kobayashi, R., & Grewal, S. I. S. (2005) · Nature Cell Biology · doi:10.1038/ncb1300 · Cited by 230 · see citing works
The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice
Tateishi, K., Omata, M., Tanaka, K., & Chiba, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104035 · Cited by 230 · see citing works
Protein neddylation and its alterations in human cancers for targeted therapy
Zhou, L., Zhang, W., Sun, Y., & Jia, L. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.01.009 · Cited by 227 · see citing works
Self-citationBasis for a ubiquitin-like protein thioester switch toggling E1–E2 affinity
Huang, D. T. C., Hunt, H. W., Zhuang, M., Ohi, M. D., Holton, J. M., & Schulman, B. A. (2007) · Nature · doi:10.1038/nature05490 · Cited by 227 · see citing works
Metabolic drivers of non-alcoholic fatty liver disease
Bence, K. K., & Birnbaum, M. J. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101143 · Cited by 223 · see citing works
Autophagy and cancer drug resistance in dialogue: Pre-clinical and clinical evidence
Qin, Y., Ashrafizadeh, M., Mongiardini, V., Grimaldi, B., Crea, F., Rietdorf, K., Győrffy, B., Klionsky, D. J., Ren, J. T., Zhang, W., et al. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216307 · Cited by 214 · see citing works
Blattner, C., Sparks, A., & Lane, D. P. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3704 · Cited by 213 · see citing works
Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome
Cavadini, S., Fischer, E. S., Bunker, R. D., Potenza, A., Lingaraju, G. M., Goldie, K. N., Mohamed, W. I., Faty, M., Petzold, G., Beckwith, R. E. J., et al. (2016) · Nature · doi:10.1038/nature17416 · Cited by 213 · see citing works
Specific and Covalent Targeting of Conjugating and Deconjugating Enzymes of Ubiquitin-Like Proteins
Hemelaar, J., Borodovsky, A., Kessler, B. M., Reverter, D., Cook, J. D., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Gill, G., Lima, C. D., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.84-95.2004 · Cited by 212 · see citing works
Active site remodelling accompanies thioester bond formation in the SUMO E1
Olsen, S. K., Capili, A. D., Lu, X., Tan, D. S., & Lima, C. D. (2010) · Nature · doi:10.1038/nature08765 · Cited by 210 · see citing works
Whitby, F. G., Xia, G., Pickart, C. M., & Hill, C. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34983 · Cited by 210 · see citing works
Functional characterization of SOX2 as an anticancer target
Zhang, S., Xiong, X., & Sun, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00242-3 · Cited by 208 · see citing works
Self-citationNEDP1, a Highly Conserved Cysteine Protease That deNEDDylates Cullins
Mendoza, H. M., Shen, L., Botting, C. H., Lewis, A., Chen, J., Ink, B. S., & Hay, R. T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212948200 · Cited by 207 · see citing works
Identification and Characterization of DEN1, a Deneddylase of the ULP Family
Gan‐Erdene, T., Kolli, N., Yin, L., Wu, K. K.-Y., Pan, Z., & Wilkinson, K. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302890200 · Cited by 204 · see citing works
Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family
Cui, J., Yao, Q., Li, S., Ding, X., Lu, Q., Mao, H., Liu, L., Zheng, N., Chen, S., & Shao, F. (2010) · Science · doi:10.1126/science.1193844 · Cited by 203 · see citing works
Structural Basis for Recruitment of Ubc12 by an E2 Binding Domain in NEDD8's E1
Huang, D. T. C., Paydar, A., Zhuang, M., Waddell, M. B., Holton, J. M., & Schulman, B. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.020 · Cited by 202 · see citing works
Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway
Yunus, A. A., & Lima, C. D. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1104 · Cited by 202 · see citing works
Xie, P., Zhang, M., He, S., Lu, K.-F., Chen, Y., Xing, G., Lu, Y.-M., Liu, P., Li, Y., Wang, S., et al. (2014) · Nature Communications · doi:10.1038/ncomms4733 · Cited by 202 · see citing works
FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity
Abida, W. M., Nikolaev, A. Y., Zhao, W., Zhang, W., & Gu, W. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609001200 · Cited by 201 · see citing works
Scott, D. C., Sviderskiy, V. O., Monda, J. K., Lydeard, J. R., Cho, S. E., Harper, J. W., & Schulman, B. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.037 · Cited by 201 · see citing works
Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation
Kurz, T., Chou, Y.-C., Willems, A. R., Meyer‐Schaller, N., Hecht, M.-L., Tyers, M., Peter, M., & Sicheri, F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.012 · Cited by 200 · see citing works
Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
Merlet, J., Burger, J., Gomes, J., & Pintard, L. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8712-7 · Cited by 197 · see citing works
Duan, S., Skaar, J. R., Kuchay, S., Toschi, A., Kanarek, N., Ben‐Neriah, Y., & Pagano, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.005 · Cited by 194 · see citing works
Overactivated Neddylation Pathway as a Therapeutic Target in Lung Cancer
Li, L., Wang, M., Yu, G., Chen, P., Li, H., Wei, D., Zhu, J. Y., Xie, L., Jia, H., Shi, J.-Y., et al. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju083 · Cited by 193 · see citing works
Self-citationProteostasis in cardiac health and disease
Henning, R. H., & Brundel, B. J. J. M. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.89 · Cited by 193 · see citing works
Wu, K. K.-Y., Yamoah, K., Dolios, G., Gan‐Erdene, T., Tan, P., Chen, A., Lee, C.-G., Wei, N., Wilkinson, K. D., Wang, R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302888200 · Cited by 192 · see citing works
Shah, J. J., Jakubowiak, A. J., O’Connor, O. A., Orlowski, R. Z., Harvey, R. D., Smith, M. R., Lebovic, D. J., Diefenbach, C., Kelly, K. R., Hua, Z., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1237 · Cited by 190 · see citing works
The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae
Kurz, T., Özlü, N., Rudolf, F., O’Rourke, S. M., Luke, B., Hofmann, K., Hyman, A. A., Bowerman, B. A., & Peter, M. (2005) · Nature · doi:10.1038/nature03662 · Cited by 188 · see citing works
Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
Horn-Ghetko, D., Krist, D. T., Prabu, J. R., Baek, K., Mulder, M. P. C., Klügel, M., Scott, D. C., Ovaa, H., Kleiger, G., & Schulman, B. A. (2021) · Nature · doi:10.1038/s41586-021-03197-9 · Cited by 187 · see citing works
NEDD8 Pathways in Cancer, Sine Quibus Non
Watson, I. R., Irwin, M. S., & Ohh, M. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.002 · Cited by 183 · see citing works
Ablation of Fbxw7 Eliminates Leukemia-Initiating Cells by Preventing Quiescence
Takeishi, S., Matsumoto, A., Onoyama, I., Naka, K., Hirao, A., & Nakayama, K. I. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.026 · Cited by 177 · see citing works
Oved, S., Mosesson, Y., Zwang, Y., Santonico, E., Shtiegman, K., Marmor, M. D., Kochupurakkal, B. S., Katz, M., Lavi, S., Cesareni, G., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513034200 · Cited by 175 · see citing works
Ribosomal proteins are targets for the NEDD8 pathway
Xirodimas, D. P., Sundqvist, A., Nakamura, A., Shen, L., Botting, C. H., & Hay, R. T. (2008) · EMBO Reports · doi:10.1038/embor.2008.10 · Cited by 175 · see citing works
Sarantopoulos, J., Shapiro, G. I., Cohen, R. B., Clark, J. W., Kauh, J. S. W., Weiss, G. J., Cleary, J. M., Mahalingam, D., Pickard, M. D., Faessel, H. M., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1338 · Cited by 169 · see citing works
Cleavage of the C-Terminus of NEDD8 by UCH-L3
Wada, H., Kito, K., Caskey, L. S., Yeh, E. T. H., & Kamitani, T. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9532 · Cited by 169 · see citing works
SREBP-1c and lipogenesis in the liver: an update
Ferré, P., Phan, F., & Foufelle, F. (2021) · Biochemical Journal · doi:10.1042/bcj20210071 · Cited by 168 · see citing works
Neddylation of PTEN regulates its nuclear import and promotes tumor development
Xie, P., Peng, Z., Chen, Y., Li, H., Du, M., Tan, Y., Zhang, X., Lü, Z., Cui, C., Liu, C. H., et al. (2020) · Cell Research · doi:10.1038/s41422-020-00443-z · Cited by 166 · see citing works
Wei, D., Li, H., Yu, J., Sebolt, J. T., Zhao, L., Lawrence, T. S., Smith, P. G., Morgan, M. A., & Sun, Y. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-2866 · Cited by 165 · see citing works
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Molecular principles underlying aggressive cancers
Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02129-7 · Cited by 86 · see citing works
Zhou, Q., Yu, H., Chen, Y., Ren, J., Lü, Y., & Sun, Y. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320655121 · Cited by 64 · see citing works
Self-citationPromising Therapeutic Strategies for Hematologic Malignancies: Innovations and Potential
Lica, J. J., Pradhan, B., Safi, K., Jakóbkiewicz‐Banecka, J., & Hellmann, A. (2024) · Molecules · doi:10.3390/molecules29174280 · Cited by 27 · see citing works
Post-Translational Modifications of Proteins Orchestrate All Hallmarks of Cancer
Bruno, P. S., Arshad, A., Gogu, M.-R., Waterman, N., Flack, R., Dunn, K., Darie, C. C., & Neagu, A.-N. (2025) · Life · doi:10.3390/life15010126 · Cited by 26 · see citing works
The Double-Edged Effects of MLN4924: Rethinking Anti-Cancer Drugs Targeting the Neddylation Pathway
Tang, H., Pang, X., Li, S., & Tang, L. (2024) · Biomolecules · doi:10.3390/biom14070738 · Cited by 24 · see citing works
Lysine: Sources, Metabolism, Physiological Importance, and Use as a Supplement
Holeček, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26188791 · Cited by 21 · see citing works
Sun, M., Ji, Y., Zhang, G., Li, Y., Dong, F., & Wu, T. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117147 · Cited by 23 · see citing works
RHEB neddylation by the UBE2F-SAG axis enhances mTORC1 activity and aggravates liver tumorigenesis
Zhang, F.-W., Xiong, X., Li, Z., Wang, H.-B., Wang, W.-L., Zhao, Y.-C., & Sun, Y. (2025) · EMBO Journal · doi:10.1038/s44318-024-00353-5 · Cited by 14 · see citing works
Self-citationWang, K., He, W., Gong, Z., Gao, J., Gao, T., Pan, N., Wu, D., Yang, Y., Li, Z., Zhao, X., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00968-1 · Cited by 14 · see citing works
Self-citationUnraveling sex differences in Alzheimer's disease and related endophenotypes with brain proteomes
Mei, Z., Liu, J., Bennett, D. A., Seyfried, N., Wingo, A. P., & Wingo, T. S. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70206 · Cited by 11 · see citing works
Li, Y., Duan, Q., Wang, C., Du, L., Jiang, Z., Li, S., Ruan, X., Huang, L., He, Z., Wen, C., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118884 · Cited by 11 · see citing works
Stratton, C. M., Ebadi, P., & Olsen, S. K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110415 · Cited by 11 · see citing works
Emerging involvement of CXCL13 in cancer development and progression
Argyris, D. G., Johnson, L., Hägglöf, T., Filippou, P. S., & Karagiannis, G. S. (2025) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2025.12.005 · Cited by 10 · see citing works
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Ren, H., Luan, Z., Zhang, R., Zhang, H., & Bian, C. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107532 · Cited by 10 · see citing works
Ye, P., Zhang, W., Liao, Y., Hu, T., & Jiang, C. (2025) · Physics of Life Reviews · doi:10.1016/j.plrev.2025.03.011 · Cited by 10 · see citing works
A comprehensive review on DCN1 protein, inhibitors and their therapeutic applications
He, Z., Yuan, Z., Yang, F., Zhang, J., Zhao, W. H., Qin, T., Zheng, X., & Ma, L. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134541 · Cited by 9 · see citing works
Discovery of small molecule inhibitors of neddylation catalyzing enzymes for anticancer therapy
Qin, X., Han, X., & Sun, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117356 · Cited by 9 · see citing works
Self-citationInhibiting neddylation: A new strategy for tumor therapy
Sun, J., Liu, C., Lang, C., Wang, J., Li, Q., Peng, C., Du, Z., Chen, Y., & Huang, P. Y. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101140 · Cited by 9 · see citing works
Jin, J., Zhang, R., Li, J., Gao, F., Liao, Z., Yu, Y., Wang, Y., Bucci, D. M., Xiao, M., Ma, R., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424061122 · Cited by 9 · see citing works
Self-citationNeddylation drives myofibrillogenesis in the developing heart
Littlejohn, R., Zambrano-Carrasco, J., Zou, J., Lu, Y., Liu, E., Kim, I., Jiao, K., Weintraub, N. L., Zhou, J., Li, J., et al. (2024) · The FASEB Journal · doi:10.1096/fj.202401380r · Cited by 8 · see citing works
Sochacka-Ćwikła, A., & Mą̨czyński, M. (2025) · Molecules · doi:10.3390/molecules30030666 · Cited by 8 · see citing works
The role of ubiquitin ligases in regulating immune cell functions
Marty, S., Yip, L., Wang, F., Kumar, M., & Fathman, C. G. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1625419 · Cited by 8 · see citing works
Mello-Vieira, J., & Đikić, I. (2026) · Nature reviews. Immunology · doi:10.1038/s41577-025-01239-1 · Cited by 8 · see citing works
Wu, W., Wang, X., Ma, R., Huang, S., Li, H., & Lyu, X. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101483 · Cited by 8 · see citing works
Role of UCHL3 in health and disease
Lei, H., Xu, H., & Wu, Y. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150626 · Cited by 7 · see citing works
Xu, L., Lyu, X., Wang, Y., Ni, L., Li, P., Zeng, P., Wang, Q., Chang, Y., Pan, C., Hu, Q., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2411429122 · Cited by 7 · see citing works
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Kim, Y. K., & Kim, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311552 · Cited by 7 · see citing works
Mitochondrial dysfunction and immune suppression in BRAF V600E‐mutated metastatic melanoma
de Almeida, N. P., Jánosi, Á. J., Hong, R., Rajeh, A. A., Nogueira, F. C. S., Szadai, L., Szeitz, B., Plá, I., Doma, V., Woldmar, N., et al. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1773 · Cited by 7 · see citing works
Survey of the human proteostasis network: the ubiquitin-proteasome system
Elsasser, S., Powers, E. T., Stoeger, T., Sui, X., Kurtzbard, R. D., Martínez-Botía, P., Wangeline, M. A., Gama, A. R., Huttlin, E. L., Elia, L. P., et al. (2026) · Autophagy · doi:10.64898/2026.03.13.711689 · Cited by 11 · see citing works
Prebiotic Peptide Synthesis: How Did Longest Peptide Appear?
Yang, Y., Wang, Z., Bai, J., & Qiao, H. (2025) · Journal of Molecular Evolution · doi:10.1007/s00239-025-10237-9 · Cited by 7 · see citing works
Adipose cullin 3 mediates the antiobesity effect of pan neddylation inhibitors
Gu, L., Du, Y., Hasan, M. N., Clayton, Y., & Li, T. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2515947122 · Cited by 6 · see citing works
Wang, Z., Sun, S., Huang, L., Chen, X., Xu, H., Ma, H., Xiao, M., & Wang, L. (2025) · Biomolecules and Biomedicine · doi:10.17305/bb.2024.11738 · Cited by 7 · see citing works
Sun, W., Li, M., Yang, Y., Dong, Q.-Q., Tao, H., Lu, C., & Yang, H. J. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107825 · Cited by 6 · see citing works
SUMOylation of the lysine-less tumor suppressor p14ARF counters ubiquitylation-dependent degradation
Motiam, A. E., Bouzaher, Y. H., Chen, H., Seoane, R., Vidal, S., Blanquer, M., Tolosa, R. M., Rodríguez-Lemus, B., Herrera-Gavilán, J. A., Vidal, A., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07854-z · Cited by 5 · see citing works
Aiello, F. A., D’Archivio, L., Attili, M., Ferraro, E., Macrì, E., Mazzocchi, R., Cassandri, M., Pomella, S., Tocco, V., Pezzullo, M., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02787-0 · Cited by 5 · see citing works
Mapping the architecture of protein complexes in Arabidopsis using cross-linking mass spectrometry
Trinh, C. S., Shrestha, R., Mao, P.-Z., Conner, W. C., Reyes, A. V., Karunadasa, S. S., Yu, A.-N., Liu, G., Hu, K., & Xu, S.-L. (2025) · bioRxiv · doi:10.1073/pnas.2519615123 · Cited by 4 · see citing works
The dual nature of KLHL proteins: From cellular regulators to disease drivers
Giulio, V. D., Canciello, A., Carletti, E., Luca, A. D., Giordano, A., Morrione, A., Berardinelli, J., Russo, V., Solari, D., Cavallo, L. M., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151483 · Cited by 5 · see citing works
Loth, C., Barbault, F., Guégan, C., Lemaire, F., Contal, C., Carvalho, A., Hellé, S., Champion, M., Kerdjoudj, H., Chan‐Seng, D., et al. (2025) · Small Science · doi:10.1002/smsc.202400618 · Cited by 5 · see citing works
Zhu, L. W., Cheng, C., Li, H., Liu, J., Wu, Y., Wu, L., & Yao, H. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07696-9 · Cited by 5 · see citing works
Discovery of New Azaindole Metallo-Deubiquitinase CSN5 Inhibitors
Lei, P., Yan, Y., Jiang, Y., Wang, Y., Xiong, R., Deng, J., Zhang, H., Yang, Z., Zhang, W., Wu, J., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00184 · Cited by 4 · see citing works
Boroumand, M., Dey, A. K., Cupp-Sutton, K. A., Pierce, T. F., Tsitsipatis, D., Herman, A. B., Wu, S., & Basisty, N. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c02694 · Cited by 3 · see citing works
Clark, M. E., Farinha, A., Morrison, A., & Lisi, G. P. (2025) · NAR Molecular Medicine · doi:10.1093/narmme/ugaf002 · Cited by 4 · see citing works
PTEN neddylation aggravates CDK4/6 inhibitor resistance in breast cancer
Liu, F., Liu, W., Tan, Y., Shang, Y., Ling, S., Jiang, X., Zhang, Z., Sun, S., & Xie, P. (2025) · Oncogene · doi:10.1038/s41388-025-03468-z · Cited by 4 · see citing works
Mukherjee, A., Vankamamidi, S. E., & Mukunthan, K. S. (2025) · Scientific Reports · doi:10.1038/s41598-025-11473-1 · Cited by 4 · see citing works
Neddylation: from regulatory mechanisms to clinical implications in cancer
Zhang, M., Peng, Q., Feng, Y., Yang, T., Yao, W., Deng, Z., & Wang, J. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.11.010 · Cited by 4 · see citing works
SMURF1: a promising target for colon cancer therapy
Xiong, X., Zhao, Y., & Sun, Y. (2024) · Protein & Cell · doi:10.1093/procel/pwae053 · Cited by 4 · see citing works
Self-citationLi, X., Zhang, Z., Xie, J., Guo, W., Deng, Z., & Huang, Z.-Y. (2025) · Arthritis & Rheumatology · doi:10.1002/art.43311 · Cited by 4 · see citing works
Cai, Z., Wu, H., Jiang, T., Ma, A., Meng, Z., Zhu, J., Lin, H., Liang, Y., Zhang, G., & Tan, M. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00037 · Cited by 3 · see citing works
Yu, H., Zhou, Q., Chen, Y., Zhong, C., Fu, T., Xiong, X., Zhu, F., Wang, L., & Sun, Y. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110575 · Cited by 3 · see citing works
Self-citationYang, G., Xiao, J., He, H., Wang, J., Wang, Z., Jian, L., & Chen, Q. (2025) · ImmunoTargets and Therapy · doi:10.2147/itt.s532644 · Cited by 3 · see citing works
Peng, K., Chen, J.-L., Hsieh, Y.-C., Hsiao, C.-Y., Yang, C.-C., Liu, J., Lee, C., Chiang, Y., & Chang, P. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118622 · Cited by 3 · see citing works
Oncogenic KRAS/ERK/JUNB signaling suppresses differentiation regulator GATA6 in pancreatic cancer
Zhong, Z., Cao, X., Liao, P.-J., Sethi, R., Klomp, J. A., Stalnecker, C. A., Chen, J., Wan, Y., Der, C. J., & Virshup, D. M. (2025) · Journal of Clinical Investigation · doi:10.1172/jci191370 · Cited by 3 · see citing works
Lv, X., Xue, J., Zhou, J., Zhao, Q., Liu, Y., Wang, L., Jiao, Y., & Qin, S. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-025-07641-6 · Cited by 3 · see citing works
邓娜, Sun, Q., Yu, X., Li, T., Sun, J., Jia, S., Ma, S., Liu, W., & Zhou, H. (2026) · Cell Death and Disease · doi:10.1038/s41419-025-08255-y · Cited by 3 · see citing works
The Role of Neddylation in Malaria Parasites
Paul, P., Nayak, B., & Mishra, S. (2024) · DNA and Cell Biology · doi:10.1089/dna.2024.0120 · Cited by 3 · see citing works
Pratummanee, K., Kerdkumthong, K., Roytrakul, S., Tantimetta, P., Runsaeng, P., Saeheng, S., & Obchoei, S. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13322 · Cited by 3 · see citing works
Luo, S., Qi, Z., Wu, F., Tao, D., Huang, S., Shi, C., Yang, C., Shi, Y., & Luo, Y. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110508 · Cited by 3 · see citing works
The Roles of E3 Ubiquitin Ligases in Cerebral Ischemia–Reperfusion Injury
Li, M., Yu, X., Liu, Q., Fang, Z. H., & Wang, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146723 · Cited by 3 · see citing works
He, J., Zou, X., Wang, D., Zhou, L., Li, X.-M., Ma, S., Shen, X., Liu, S., & Liu, B. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167985 · Cited by 3 · see citing works
Ubiquitin-like Proteins in Autoimmune Diseases: Current Evidence and Therapeutic Opportunities
Lee, B., Jeong, H., Kim, Y.-R., Roh, J. S., & Sohn, D. H. (2025) · Immune Network · doi:10.4110/in.2025.25.e21 · Cited by 3 · see citing works
Pan-cancer analysis unveils the role and mechanisms of neddylation modifications in tumorigenesis
Hu, Q., Li, X., Wang, P., & Xie, Y. (2025) · Medical Oncology · doi:10.1007/s12032-025-02658-9 · Cited by 2 · see citing works
E3 Ligase Rbx1 Orchestrates Thymus Development and Fate Determination of αβ-γδ T Cells
Wu, D., Chen, Q., Tan, M., & Sun, Y. (2025) · Research · doi:10.34133/research.0774 · Cited by 2 · see citing works
Self-citationGuo, X., Ke, Y., Chen, Y., Li, Y., Zhang, J., Zheng, W., Feng, P., Ji, Y., Wang, Z., Lu, Y., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110511 · Cited by 2 · see citing works
Zheng, Z., Zhao, F., Zhao, S., Bai, Y., Shi, L., Zhu, B., Huang, X., Zheng, Y., Zhao, Q., Wen, Y., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.150018 · Cited by 2 · see citing works
Yuan, Z., Wang, Z., Qin, T., & Yu, B. (2026) · Targetome · doi:10.48130/targetome-0025-0013 · Cited by 2 · see citing works
Li, Y.-R., Chiang, P., Hou, S.-Y., Lin, C., Lo, L., & Fu, S. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109946 · Cited by 2 · see citing works
CRL3 E3 ligase regulates glutamine and cystine metabolisms
Zhou, Q., Li, Z., & Sun, Y. (2024) · Protein & Cell · doi:10.1093/procel/pwae051 · Cited by 2 · see citing works
Self-citationInhibition of cardiomyocyte neddylation impairs embryonic cardiac morphogenesis
Littlejohn, R., Zambrano-Carrasco, J., Zou, J., Yao, Y., Kim, I., Zhou, J., Li, J., & Su, H. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.10.006 · Cited by 2 · see citing works
Halilovic, M., Abdelsalam, M. A. M., Mieland, A. O., Neuroth, S., Ashry, R., Zabkiewicz, J., Lazenby, M., Alvares, C. L., Schmidt, M., Brenner, W., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.20.660791 · Cited by 2 · see citing works
Shen, W., Guo, F., Jiang, H., Gao, J., Chen, W., Yu, Z., Yuan, J., Huang, M., Zong, M., Li, M., et al. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116206 · Cited by 1 · see citing works
Zhang, H., Zhao, Z., Shi, W., Niu, G., Feng, D., Wang, M., Zhou, Z., Li, Z., Zhao, J., & Wu, Y. (2025) · Postgraduate Medical Journal · doi:10.1093/postmj/qgaf125 · Cited by 1 · see citing works
Self-citationGencel‐Augusto, J., Grandis, J. R., & Johnson, D. E. (2025) · Advances in Biological Regulation · doi:10.1016/j.jbior.2025.101117 · Cited by 1 · see citing works
Decorin Evokes a Pro‐Lysosomal Pathway in Lymphatic Endothelial Cells
Pascal, G. J., Mondal, D. K., Kim, S., Xie, C., Sankar, D. S., Dengjel, J., & Iozzo, R. V. (2025) · Proteoglycan Research · doi:10.1002/pgr2.70038 · Cited by 1 · see citing works
HIV proviral transcription and infectivity are enhanced by neddylation
Vaca, C. C., Hudson, H., Clerc, I., Song, C., & D’Aquila, R. T. (2025) · Journal of Virology · doi:10.1128/jvi.00968-25 · Cited by 1 · see citing works
Wang, X., Zhang, H., & Wang, J. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1654064 · Cited by 1 · see citing works
Cui, D., Qu, R., Li, T., Wang, L., Chen, X., Shao, S., Liang, X., Xu, J., Sun, Y., Xiong, X., et al. (2025) · Advanced Science · doi:10.1002/advs.202512652 · Cited by 1 · see citing works
Self-citationEcological History Shapes Transcriptome Variation in Quiescent Saccharomyces cerevisiae
Marek, A., Tomala, K., & Wloch‐Salamon, D. (2025) · Biomolecules · doi:10.3390/biom15111588 · Cited by 1 · see citing works
Zhou, Y., Tao, S., Liu, L.-J., & Zhang, L. (2025) · Biomedicines · doi:10.3390/biomedicines13122873 · Cited by 2 · see citing works
Mitsiadou, D., Xirodimas, D. P., & Polanowska, J. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253036 · Cited by 1 · see citing works
Wei, J., Cheng, K., Wu, X., Zhang, L., Wang, Q., Liang, Y., Zhu, Z., Meng, W., Chen, W., Guan, X., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08320-6 · Cited by 1 · see citing works
Du, X.-R., Gao, Y., Zeng, Q., Zhang, G., & Liu, W. (2025) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2025.195132 · Cited by 1 · see citing works
Zhu, Z., Zhang, X., Wang, S., Huang, Y., Han, X., Lai, D., Yao, X., Lan, W., Nong, H., Zeng, W., et al. (2025) · Discover Oncology · doi:10.1007/s12672-025-04340-y · Cited by 1 · see citing works
Felix-Lopez, A., López-Orozco, J., Elaish, M., Fayad, N., Xu, Z., Woldemariam, T. A., Hassan, B. B., Panigrahi, R. R., Khan, J. Q., Rohamare, M., et al. (2025) · iScience · doi:10.1016/j.isci.2025.114566 · Cited by 1 · see citing works
Role of neddylation in diabetes metabolism: potential therapeutic target
Li, H., Zeng, R., Liu, J., & Wang, H. (2026) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-025-01837-9 · Cited by 1 · see citing works
Rao, W., Huang, Y., Li, J., Chen, Q., Sun, J., & Huang, L. (2026) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2026.108582 · Cited by 2 · see citing works
UFMylation: biological mechanisms, functions, and clinical implications
Wu, X., Yuan, Q., & Yin, Q. (2026) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2026.02.014 · Cited by 1 · see citing works
Chen, T., Zhou, J.-X., Hou, Y.-R., Zhang, Y.-N., Li, C., Zhu, J., Guo, Z., & Cui, Y. (2026) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.67.3.5 · Cited by 1 · see citing works
A guide to mapping ubiquitin and ubiquitin‐like E3 ligases to their substrates
Merino‐Cacho, L., Guinea-Pérez, C., Pozo-Rodríguez, M., Cano-López, S., Ramírez, J., Barroso‐Gomila, O., Mayor, U., Sutherland, J. D., & Barrio, R. (2026) · FEBS Journal · doi:10.1111/febs.70479 · Cited by 3 · see citing works
UBE2M promotes malignant phenotypes of prostate cancer through mediating NAA10 neddylation
Wang, Q., Zhang, J. L., Lin, X., Shi, R., Pan, C., Hu, Q., Xu, L., Chen, Q., Xue, D., Yin, J., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08001-8 · Cited by 1 · see citing works
Ubiquitin-like modifications in adipose tissue development and obesity: New insights
Chakraborty, S., & Chen, W. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168234 · Cited by 1 · see citing works
Guo, W., Fan, M., Sun, Z., Huang, H., Mo, G., Luo, Z., Xu, J., Liang, L., & Wang, S. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152019 · Cited by 1 · see citing works
Neddylation of STAT3 is a potential therapeutic target for MASLD
Liu, F., Zhao, F., Du, M., Ma, J., Shang, Y., Liu, Z., Zhu, Y., Zhang, Z., & Xie, P. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168261 · Cited by 1 · see citing works
Hu, Y., Shan, Z., Sun, X., Liang, J., Wang, L., Zhou, X., & Chen, X. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152388 · Cited by 1 · see citing works
Chang, Y., Qiao, C., Xu, X., Lyu, X., Xu, L., Hu, Q., Han, Y., Wu, Y., Zhang, X., Li, Q., et al. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08881-0 · Cited by 1 · see citing works
Xu, N., Shao, J., Jiang, L., Zhao, H., & Zheng, W. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189653 · Cited by 1 · see citing works
Protein neddylation as a therapeutic target: challenges and opportunities
Zhang, S., Lan, H., & Sun, Y. (2026) · Journal of Clinical Investigation · doi:10.1172/jci206924 · Cited by 1 · see citing works
Self-citationZheng, Y., Chen, C. F., Li, X., Li, Z., Li, H., Tan, M., Zhai, D., Zhang, F., Lü, W., 陈志华, et al. (2026) · 中国科学通报:英文版 · doi:10.1016/j.scib.2026.08.050 · Cited by 1 · see citing works
Self-citationGill regeneration in the mayfly Cloeon uncovers new molecular pathways in insect regeneration
Martín-Blanco, C. A., Navarro, P., Esteban-Collado, J., Serras, F., Almudí, I., & Casares, F. (2024) · Open Biology · doi:10.1098/rsob.240118 · Cited by 1 · see citing works
Pan, Y., Dai, J., Liu, Y., Wang, Y., Zhang, Q., Lou, Y., & Qiu, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143539 · Cited by 1 · see citing works
Neddylation Regulates Mitochondrial Dynamics and Turnover in the Adult HeartPreprint
Zou, J., Wang, W., Chen, Q., Zhang, L., Zambrano-Carrasco, J., Li, Y., Lu, Y., Zhou, H., Dong, K., Fukai, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.03.692150 · Cited by 1 · see citing works
- Authors
- Zhang, S., Yu, Q., Li, Z., Zhao, Y., & Sun, Y.
- Affiliations
- Second Affiliated Hospital of Zhejiang University (CN)
- Chinese Academy of Sciences (CN)
- First Affiliated Hospital Zhejiang University (CN)
- Corresponding author
- Zhao, Yongchao
- Sun, Yi
- Venue
- Signal Transduction and Targeted Therapy
- Published
- 2024-04-05
- Volume
- 9
- Issue
- 1
- Pages
- 85-85
- ISSN
- 2059-3635 (ISSN-L)
- PMC
- PMC10995212
- OpenAlex
- W4393952844
- Cited by
- 171
- References
- 537
- Citations by year
- 2026: 78 · 2025: 74 · 2024: 19
- FWCI
- 6.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Signal Transduction and Targeted Therapy (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (U22A20317, 82202838, 82102749, 92053117, 81972591)
- Natural Science Foundation of Zhejiang Province (LD22H300003, LZ22H160003)
- The National Key R&D Program of China
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- NEDD8, cullin neddylation, cullin-RING ligases, E3 ubiquitin ligase, neddylation inhibitor, cancer, metabolic disorders, neurodegenerative diseases, liver dysfunction, small molecule inhibitors
- MeSH terms
- Humans, Neoplasms, Protein Processing, Post-Translational, Ubiquitins, Ubiquitin-Protein Ligases, Cullin Proteins
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