Ubiquitination in disease pathogenesis and treatment

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882

Type 2 diabetes as an inflammatory disease

Donath, M. Y., & Shoelson, S. E. (2011) · Nature Reviews Immunology · doi:10.1038/nri2925 · Cited by 3,737

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012

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

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347

Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene

Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311

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

Mutations of the VHL tumour suppressor gene in renal carcinoma

Gnarra, J. R., Tory, K., Weng, Y., Schmidt, L., Wei, M. H., Li, H., Latif, F., Liu, S., Chen, F., Duh, F.-M., et al. (1994) · Nature Genetics · doi:10.1038/ng0594-85 · Cited by 1,730

Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583

Cellular quality control by the ubiquitin–proteasome system and autophagy

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

Post-translational modifications in proteins: resources, tools and prediction methods

Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 772

Structural insights into the catalysis and regulation of E3 ubiquitin ligases

Buetow, L., & Huang, D. T. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.91 · Cited by 679

Advancing targeted protein degradation for cancer therapy

Dale, B., Cheng, M., Park, K.-S., Kaniskan, H. Ü., Xiong, Y., & Jin, J. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-021-00365-x · Cited by 632

The role of ubiquitination and deubiquitination in cancer metabolism

Sun, T., Liu, Z., & Yang, Q. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01262-x · Cited by 508

Elusive roles for reactive astrocytes in neurodegenerative diseases

Ben Haim, L., Carrillo-de Sauvage, M.-A., Ceyzériat, K., & Escartin, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00278 · Cited by 453

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442

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

An Overview of the Role of Lipofuscin in Age-Related Neurodegeneration

Moreno-García, A., Kun, A., Calero, O., Medina, M., & Calero, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00464 · Cited by 372

Post-translational regulation of ubiquitin signaling

Song, L., & Luo, Z.-Q. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201902074 · Cited by 346

UbiBrowser 2.0: a comprehensive resource for proteome-wide known and predicted ubiquitin ligase/deubiquitinase–substrate interactions in eukaryotic species

Wang, X., Li, Y., He, M., Kong, X., Jiang, P., Liu, X., Diao, L., Zhang, X., Li, H., Ling, X., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab962 · Cited by 260

The Multiple Roles of Interferon Regulatory Factor family in Health and Disease

Wang, L., Zhu, Y., Zhang, N., Xian, Y., Tang, Y., Ye, J., Reza, F., He, G., Wen, X., & Jiang, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01980-4 · Cited by 178

UBA1: At the Crossroads of Ubiquitin Homeostasis and Neurodegeneration

Groen, E. J. N., & Gillingwater, T. H. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.08.003 · Cited by 157

Bassoon proteinopathy drives neurodegeneration in multiple sclerosis

Schattling, B., Engler, J. B., Volkmann, C., Rothammer, N., Woo, M. S., Petersen, M., Winkler, I., Kaufmann, M., Rosenkranz, S. C., Fejtova, A., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0385-4 · Cited by 86

Endosomal trafficking in metabolic homeostasis and diseases

Gilleron, J., & Zeigerer, A. (2023) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00737-9 · Cited by 57

Targeting post-translational modification of transcription factors as cancer therapy

Qian, M., Yan, F., Yuan, T., Yang, B., He, Q., & Zhu, H. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.06.005 · Cited by 47

Inhibition of USP1 Activates ER Stress through Ubi-Protein Aggregation to Induce Autophagy and Apoptosis in HCC

Wang, L., Hu, T., Shen, Z., Zheng, Y., Geng, Q., Li, L., Sha, B., Li, M., Sun, Y., Guo, Y., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05341-3 · Cited by 45

Cyanopyrrolidine inhibitors of ubiquitin specific protease 7 mediate desulfhydration of the active-site cysteine.

Bashore, C., Jaishankar, P., Skelton, N. J., Fuhrmann, J., Hearn, B. R., Liu, P. S., Renslo, A. R., & Dueber, E. C. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00031 · Cited by 34

Structural basis for the midnolin-proteasome pathway and its role in suppressing myeloma

Nardone, C., Gao, J., Seo, H.-S., Mintseris, J., Ort, L., Yip, M. C. J., Negasi, M., Besschetnova, A. K., Kamitaki, N., Gygi, S. P., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.05.030 · Cited by 22

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

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

All roads lead to ubiquitin

Gyrd-Hansen, M. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.93 · Cited by 15

Structural insights into ubiquitin chain cleavage by Legionella ovarian tumor deubiquitinases

Kang, S., Kim, G., Choi, M., Jeong, M., van der Heden van Noort, G. J., Roh, S.-H., & Shin, D. (2023) · Life Science Alliance · doi:10.26508/lsa.202201876 · Cited by 9

Loss-of-function mutations in the dystonia gene THAP1 impair proteasome function by inhibiting PSMB5 expression

Ramage, D. E., Grant, D. W., & Timms, R. T. (2025) · Nature Communications · doi:10.1038/s41467-025-56782-1 · Cited by 6

Cleavage‐Resistant CYLD Protects Against Autoimmune Hepatitis

Liu, H., Su, C., Liu, J., Xing, M., Wu, X., Wang, L., Zhao, X., Zhang, H., Xie, Y., Wang, Y., et al. (2026) · Advanced Science · doi:10.1002/advs.202513015 · Cited by 1