Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

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Function and regulation of cullin–RING ubiquitin ligases

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Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb

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Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

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Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress

Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480

SKP1 Connects Cell Cycle Regulators to the Ubiquitin Proteolysis Machinery through a Novel Motif, the F-Box

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Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex

Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,284

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

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Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression

McMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300931200 · Cited by 1,141

The SCF ubiquitin ligase: insights into a molecular machine

Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114

The E3 ubiquitin ligase mechanism specifying targeted microRNA degradation

Farnung, J., Slobodyanyuk, E., Wang, P. Y., Blodgett, L. W., Lin, D. H., von Gronau, S., Schulman, B. A., & Bartel, D. P. (2026) · Nature · doi:10.1038/s41586-026-10232-0 · Cited by 14

Reduction of oligomer size modulates the competition between cluster formation and phase separation of the tumor suppressor SPOP

Sabri, N., Cuneo, M. J., Marzahn, M. R., Lee, J., Bouchard, J. J., Güllülü, Ö., Vaithiyalingam, S., Borgia, M. B., Schmit, J. D., & Mittag, T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105427 · Cited by 14

Proteolysis-targeting influenza vaccine strains induce broad-spectrum immunity and in vivo protection

Shen, J., Li, J., Shen, Q., Hou, J., Zhang, C., Bai, H., Ai, X., Su, Y., Wang, Z., Zhang, Y., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01908-2 · Cited by 14

Identification of SPOP related metabolic pathways in prostate cancer

Yan, M., Qi, H., Li, J., Ye, G., Shao, Y., Li, T., Liu, J., Piao, H., & Xu, G. (2017) · Oncotarget · doi:10.18632/oncotarget.21460 · Cited by 14

SPOP Deregulation Improves the Radiation Response of Prostate Cancer Models by Impairing DNA Damage Repair

Bezawy, R. E., Tripari, M., Percio, S., Cicchetti, A., Tortoreto, M., Stucchi, C., Tinelli, S., Zuco, V., Doldi, V., Gandellini, P., et al. (2020) · Cancers · doi:10.3390/cancers12061462 · Cited by 14

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

Crystal structure of the UBR‐box from UBR6/FBXO11 reveals domain swapping mediated by zinc binding

Muñoz‐Escobar, J., Kozlov, G., & Gehring, K. (2017) · Protein Science · doi:10.1002/pro.3227 · Cited by 14

Deficiency of Cullin 3, a Protein Encoded by a Schizophrenia and Autism Risk Gene, Impairs Behaviors by Enhancing the Excitability of Ventral Tegmental Area (VTA) DA Neurons

Gao, N., Liu, Z., Wang, H., Shen, C., Dong, Z., Cui, W., Xiong, W., & Mei, L. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0247-23.2023 · Cited by 14

ELK3 destabilization by speckle-type POZ protein suppresses prostate cancer progression and docetaxel resistance

Lee, C., Lee, H.-J., Kim, S., Nam, S.-B., Lee, G.-E., Yang, K. E., Lee, G. J., Chun, S. H., Kang, H. C., Lee, J. Y., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06647-0 · Cited by 13

Snail promotes prostate cancer migration by facilitating SPOP ubiquitination and degradation

Lv, W., Huan, M., Yang, W., Gao, Y., wang, K., Xu, S., Zhang, M., Ma, J., Wang, X., Chen, Y., et al. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.187 · Cited by 13

ETS Fusion Genes in Prostate Cancer

Brenner, J. C., Chinnaiyan, A. M., & Tomlins, S. A. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6828-8_5 · Cited by 13

Molecular Underpinnings Governing Genetic Complexity of ETS-Fusion-Negative Prostate Cancer

Bhatia, V., & Ateeq, B. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.001 · Cited by 14

Biomolecular condensates: A new lens on cancer biology

Jiang, L., & Kang, Y. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189245 · Cited by 13

Ubiquitin ligases and medulloblastoma: genetic markers of the four consensus subgroups identified through transcriptome datasets

Vriend, J. P., & Rastegar, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165839 · Cited by 12

Expression and purification of functional recombinant CUL2•RBX1 from E. coli

Diaz, S., Li, L., Wang, K., & Liu, X. (2021) · Scientific Reports · doi:10.1038/s41598-021-90770-x · Cited by 14

Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1

Orth, B., Sander, B., Möglich, A., Diederichs, K., Eilers, M., & Lorenz, S. (2021) · Structure · doi:10.1016/j.str.2021.06.005 · Cited by 12

Discovery and identification of a novel small molecule BCL-2 inhibitor that binds to the BH4 domain

Zhou, J., Yang, R., Chang, J., Song, J., Fan, Z., Zhang, Y., Lu, C.-H., Jiang, H., Zheng, M.-Y., & Zhang, S. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00936-0 · Cited by 13

Lessons from tissue compartment-specific analysis of androgen receptor alterations in prostate cancer

Daniel, M. L., & Dehm, S. M. (2016) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2016.04.016 · Cited by 12

Targeting SPOP with small molecules provides a novel strategy for kidney cancer therapy

Zheng, T., & Yang, C. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-0297-2 · Cited by 11

Cullin3/ KCTD 5 induces monoubiquitination of ΔNp63α and impairs its activity

He, H., Peng, Y., Fan, S., Chen, Y., Zheng, X., & Li, C. (2018) · FEBS Letters · doi:10.1002/1873-3468.13104 · Cited by 12

SPOP attenuates migration and invasion of choriocarcinoma cells by promoting DHX9 degradation.

Yuan, D., Chen, Y., Yang, Z., Li, G., Wu, M., Jiang, J., Li, D., & Yu, Q. (2020) · PubMed Central · Cited by 12

Ubiquitin E3 ligase SPOP is a host negative regulator of enterovirus 71-encoded 2A protease

Zang, L., Yang, X., Chen, Y., Huang, F., Yuan, Y., Chen, X., Zuo, Y., Miao, Y., Gu, J., Guo, H., et al. (2023) · Journal of Virology · doi:10.1128/jvi.00786-23 · Cited by 11

TRIM24-mediated K27-linked ubiquitination of ULK1 alleviates energy stress-induced autophagy and promote prostate cancer growth in the context of SPOP mutation

Chen, S., Lin, J., Yang, Z., Wang, Y., Wang, Q., Wang, D., Qu, Y., Lin, Q., Liu, J., Shi, Y., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01582-9 · Cited by 13

Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro

Flynn, A. J., Miller, K., Codjoe, J. M., King, M. R., Posey, A. E., & Haswell, E. S. (2023) · Plant Direct · doi:10.1002/pld3.515 · Cited by 11

Emerging Role of the Ubiquitin Proteasome System in the Control of Shoot Apical Meristem FunctionF

Giacomo, E. D., Serino, G., & Frugis, G. (2012) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12010 · Cited by 11

SPOP Is a Key Trigger of Pathological Cardiac Hypertrophy and Heart Failure

Wu, H., Zhuang, Y., Yue, Y., Liu, J., Han, J., Yao, Y., Xu, X., Liu, J., Li, Y., Yang, Z., et al. (2025) · Circulation Research · doi:10.1161/circresaha.125.326129 · Cited by 10

Structural mimicry of UM171 and neomorphic cancer mutants co-opts E3 ligase KBTBD4 for HDAC1/2 recruitment

Chen, Z., Chi, G., Balo, T., Chen, X., Montes, B. R., Clifford, S. C., D’Angiolella, V., Szabo, T., Kiss, A., Novak, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58350-z · Cited by 10

Speckle-type POZ (pox virus and zinc finger protein) protein gene deletion in ovarian cancer: Fluorescence in situ hybridization analysis of a tissue microarray

Hu, X., Yang, Z., Zeng, M., LIU, Y., Yang, X., Li, Y., Li, X. U., & Yu, Q. (2016) · Oncology Letters · doi:10.3892/ol.2016.4643 · Cited by 10

A Synopsis of Signaling Crosstalk of Pericytes and Endothelial Cells in Salivary Gland

Cucu, I., & Nicolescu, M. I. (2021) · Dentistry Journal · doi:10.3390/dj9120144 · Cited by 12

Using CRL3BPM E3 ligase substrate recognition sites as tools to impact plant development and stress tolerance in Arabidopsis thaliana

Al‐Saharin, R., Mooney, S., Dißmeyer, N., & Hellmann, H. A. (2022) · Plant Direct · doi:10.1002/pld3.474 · Cited by 10

A Novel Bipartite Nuclear Localization Signal Guides BPM1 Protein to Nucleolus Suggesting Its Cullin3 Independent Function

Leljak-Levanić, D., Horvat, T., Martinčić, J., & Bauer, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051184 · Cited by 10

Conformational and oligomeric states of SPOP from small-angle X-ray scattering and molecular dynamics simulations

Thomasen, F. E., Cuneo, M. J., Mittag, T., & Lindorff-Larsen, K. (2023) · eLife · doi:10.7554/elife.84147 · Cited by 9

SPOP Suppresses Hepatocellular Carcinoma Growth and Metastasis by Ubiquitination and Proteasomal Degradation of TRAF6

Chang, W.-Y., Feng, K., Zhou, P., Gong, D.-A., Wang, K., Huang, A.-L., Wang, K., & Tang, N. (2025) · Cancer Science · doi:10.1111/cas.70025 · Cited by 10

KCTD10 is a sensor for co-directional transcription–replication conflicts

Kloeber, J. A., Chen, B., Sun, G., King, C. S., Wang, Z., Wang, L., Wu, Z., Zhu, S., Zhao, F., Qin, H., et al. (2025) · Nature · doi:10.1038/s41586-025-09585-9 · Cited by 9

Biophysical Characterization of the Binding Mechanism between the MATH Domain of SPOP and Its Physiological Partners

Diop, A., Pietrangeli, P., Nardella, C., Pennacchietti, V., Pagano, L., Toto, A., Felice, M. D., Matteo, S. D., Marcocci, L., Malagrinò, F., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210138 · Cited by 9

The CRL3 gigaxonin ubiquitin ligase–USP15 pathway governs the destruction of neurofilament proteins

Park, H.-M., Le, L., Nguyen, T. T., Nam, K. H., Ordureau, A., Lee, J. E., & Nguyen, T. V. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2306395120 · Cited by 9

Chromatin-mediated silencing on the inactive X chromosome

Keniry, A., & Blewitt, M. E. (2023) · Development · doi:10.1242/dev.201742 · Cited by 9

E3 Ubiquitin Ligases in Cancer and Their Pharmacological Targeting

Ong, J. Y., & Torres, J. Z. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82883 · Cited by 8

Novel mutations in the 3-box motif of the BACK domain of KLHL7 associated with nonsyndromic autosomal dominant retinitis pigmentosa

Oh, J. K., de Carvalho, J. R. L., Sun, Y. J., Ragi, S. D., Yang, J., Levi, S. R., Ryu, J., Bassuk, A. G., Mahajan, V. B., & Tsang, S. H. (2019) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-019-1275-2 · Cited by 9

Determining the Effects of Neddylation on Cullin‐RING Ligase–Dependent Protein Ubiquitination

Wang, K., & Liu, X. (2022) · Current Protocols · doi:10.1002/cpz1.401 · Cited by 9

Somatic mutation ofSPOPtumor suppressor gene is rare in breast, lung, liver cancers, and acute leukemias

Kim, M. S., Kim, M., Yoo, N. J., & Lee, S. H. (2013) · Apmis · doi:10.1111/apm.12108 · Cited by 9

SPOP–PTEN–SUFU axis promotes progression of clear cell renal cell carcinoma via activating SHH and WNT pathway

Han, B., Sun, Z., Yu, T., Wang, Y., Kuang, L., Li, T., Cai, J., Cao, Q., Xu, Y., Gao, B., et al. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00484-2 · Cited by 7

A near-complete map of human cytosolic degrons and their relevance for disease

Voutsinos, V., Johansson, K. E., Larsen, F. B., Grønbæk-Thygesen, M., Jonsson, N., Holm-Olesen, E., Tesei, G., Stein, A., Fowler, D. M., Lindorff‐Larsen, K., et al. (2026) · Science Advances · doi:10.1126/sciadv.adz3483 · Cited by 12

BPM1 regulates RdDM-mediated DNA methylation via a cullin 3 independent mechanism

Jagić, M., Vuk, T., Škiljaica, A., Markulin, L., Bočkor, V. V., Tokić, M., Miškec, K., Razdorov, G., Habazin, S., Šoštar, M., et al. (2022) · Plant Cell Reports · doi:10.1007/s00299-022-02911-9 · Cited by 8

SPOP Regulates Endometrial Stromal Cell Decidualization in Mice

Liu, N., Liu, X., Yu, Q., Chen, X., Ding, Y., He, J., Gao, R., Wang, Y., & Liu, X. (2016) · Reproductive Sciences · doi:10.1177/1933719116648215 · Cited by 8

Next-Generation Sequencing

Offermann, A., & Perner, S. (2017) · Molecular pathology library · doi:10.1007/978-3-319-64096-9_12 · Cited by 8

STK31 upregulation is associated with chromatin remodeling in gastric cancer and induction of tumorigenicity in a xenograft mouse model

Bae, D. H., Kim, H., Yoon, B.-H., Park, J., Kim, S., Kim, S., Kim, S., Lee, S.-I., Song, K., & Kim, Y. Y. (2021) · Oncology Reports · doi:10.3892/or.2021.7993 · Cited by 8

The SPOP-ITCH Signaling Axis Protects Against Prostate Cancer Metastasis

Ma, J., Cai, M., Mo, Y., Fried, J. S., Tan, X., Ma, Y., Chen, J., Han, S., & Xu, B. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.658230 · Cited by 8

LMNB2-mediated high PD-L1 transcription triggers the immune escape of hepatocellular carcinoma

Li, Y., Zhu, J., Zhai, F., Ge, Y., Zhan, Z., Wang, S., Kong, L., Zhao, J., Hu, L., Wang, S., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02540-7 · Cited by 7

Xist condensates: perspectives for therapeutic intervention

Perotti, I., Broglia, L., Tartaglia, G. G., & Cerase, A. (2025) · Genome biology · doi:10.1186/s13059-025-03666-8 · Cited by 11

Dimerization of the ETO1 family proteins plays a crucial role in regulating ethylene biosynthesis in Arabidopsis thaliana

Gu, S., Lo, W., Wu, S.-J., & Wang, L. (2020) · The Plant Journal · doi:10.1111/tpj.15111 · Cited by 7

SPOP negatively regulates mTORC1 activity by ubiquitinating Sec13

Yang, Y., Han, Y., Cao, Q., Wang, X., Wei, X.-D., Shang, M.-D., Zhang, X., Li, X., Hu, B., Tian, C.-Y., et al. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111060 · Cited by 8

Mutation in histone deacetylase HDA-3 leads to shortened locomotor healthspan in Caenorhabditis elegans

Kawamura, K., & MARUYAMA, I. N. (2020) · Aging · doi:10.18632/aging.202296 · Cited by 7

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

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

The dynamics of the β-propeller domain in Kelch protein KLHL40 changes upon nemaline myopathy-associated mutation

Lambrughi, M., Lucchini, M., Pignataro, M., Sola, M., & Bortolotti, C. A. (2016) · RSC Advances · doi:10.1039/c6ra06312h · Cited by 6

Expression and clinical relevance of SPOPL in medulloblastoma

Hu, Y., Yang, L., Zhang, M., Huang, Z., Lin, J.-P., & Zhang, N. (2017) · Oncology Letters · doi:10.3892/ol.2017.6500 · Cited by 7

Proteasomal Degradation of Zn-Dependent Hdacs: The E3-Ligases Implicated and the Designed Protacs That Enable Degradation

Márquez-Cantudo, L., Ramos, A., Coderch, C., & de Pascual‐Teresa, B. (2021) · Molecules · doi:10.3390/molecules26185606 · Cited by 8

BTB/POZ-MATH proteins regulate Arabidopsis seedling development by promoting auxin-independent degradation of the Aux/IAA protein IAA10

Ban, Z., Hou, Y., Ku, E., Zhu, Y., Hu, Y., Karadanaian, N., Zhao, Y., & Estelle, M. A. (2025) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiaf155 · Cited by 6

Prostate Cancer Epigenetic Plasticity and Enhancer Heterogeneity: Molecular Causes, Consequences and Clinical Implications

Kneppers, J., Bergman, A. M., & Zwart, W. T. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-11836-4_15 · Cited by 6

Brassica napus Plants Gain Improved Salt-Stress Tolerance and Increased Storage Oil Biosynthesis by Interfering with CRL3BPM Activities

Corbridge, E., MacGregor, A., Al‐Saharin, R., Garneau, M. G., Smalley, S., Mooney, S., Roje, S., Bates, P. D., & Hellmann, H. A. (2023) · Plants · doi:10.3390/plants12051085 · Cited by 6

SPOP promotes CREB5 ubiquitination to inhibit MET signaling in liver cancer

Gong, D.-A., Zhou, P., Chang, W.-Y., Yang, J.-Y., Zhang, Y.-L., Huang, A., Tang, N., & Wang, K. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119642 · Cited by 6

Understanding functions of eEF1 translation elongation factors beyond translation. A proteomic approach

Negrutskii, B. S., Porubleva, L. V., Malinowska, A., Novosylna, O. V., Dadlez, M., & Knudsen, C. R. (2023) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.10.001 · Cited by 6

Dysregulation of ubiquitination modification in renal cell carcinoma

You, H., Zhang, H., Jin, X., & Yan, Z. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1453191 · Cited by 7

Deuterium labeling enables proteome-wide turnover kinetics analysis in cell culture

Alamillo, L., Ng, D. C. M., Currie, J., Black, A., Pandi, B., Manda, V., Pavelka, J., Schaal, P., Travers, J. G., McKinsey, T. A., et al. (2025) · Cell Reports Methods · doi:10.1016/j.crmeth.2025.101104 · Cited by 6

The Hh pathway promotes cell apoptosis through Ci-Rdx-Diap1 axis

Liu, B., Ding, Y., Sun, B., Liu, Q., Zhou, Z., & Zhan, M. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00653-3 · Cited by 6

Mining of the CULLIN E3 ubiquitin ligase genes in the whole genome of Salvia miltiorrhiza

Gao, X., Li, X., Chen, C., Wang, C., Fu, Y., Zheng, Z., Shi, M., Hao, X., Zhao, L., Qiu, M., et al. (2022) · Current Research in Food Science · doi:10.1016/j.crfs.2022.10.011 · Cited by 6

Template‐based structure prediction and classification of transcription factors in Arabidopsis thaliana

Lu, T., Yang, Y., Yao, B., Liu, S., Zhou, Y., & Zhang, C. (2012) · Protein Science · doi:10.1002/pro.2066 · Cited by 6

A Peptide Binder of E3 Ligase Adaptor SPOP Disrupts Oncogenic SPOP‐Protein Interactions in Kidney Cancer Cells

Wang, Z., Zhang, H., Chen, B., Ouyang, S., Zheng, T., Zhou, R., Dong, Z., Huang, Y., Zhang, T., Jiang, H., et al. (2020) · Chinese Journal of Chemistry · doi:10.1002/cjoc.202000462 · Cited by 6

SPOP inhibits BRAF-dependent tumorigenesis through promoting non-degradative ubiquitination of BRAF

Feng, K. M., Shi, Q., Jiao, D., Chen, Y., Yang, W., Su, K., Wang, Y., Huang, Y., Zhang, P., Li, Y., et al. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00950-z · Cited by 6

Crystal structure of the yeast Rad7-Elc1 complex and assembly of the Rad7-Rad16-Elc1-Cul3 complex

Liu, L., Huo, Y., Li, J., & Jiang, T. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.02.012 · Cited by 7

SPOP Regulates The Biological Mechanism Of Ovarian Cancer Cells Through The Hh Signaling Pathway

Li, Y., Yu, Q., Li, R., Luo, J., Yuan, D., Song, J., Sun, Y., Long, T., & Yang, Z. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s215940 · Cited by 6

Synthesis and Biological Evaluation of β-Lactam Derivatives Targeting Speckle-Type POZ Protein (SPOP)

Zhou, C., Hao, X., Chen, Z., Zhang, R., Zhou, Q., Fan, Z., Zheng, M., Hou, H., Zhang, S., & Guo, H. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00515 · Cited by 5

Ubiquitin Proteins and the Orchestration of Transcription Factors Activity

He, Y., Zhang, K., Georgiev, M. I., & Zhou, M. (2021) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2021.1951491 · Cited by 5

The association of speckle-type POZ protein with lymph node metastasis and prognosis in cancer patients

Cheng, F., Zeng, C., Zeng, L., Wu, C., & Chen, Y. (2019) · Medicine · doi:10.1097/md.0000000000017439 · Cited by 5

Oncoprotein ubiquitylation

Welcker, M., & Clurman, B. E. (2014) · Cell Cycle · doi:10.4161/cc.29325 · Cited by 5

A complete map of human cytosolic degrons and their relevance for diseasePreprint

Voutsinos, V., Johansson, K. E., Larsen, F. B., Grønbæk-Thygesen, M., Jonsson, N., Holm-Olesen, E., Tesei, G., Stein, A., Fowler, D. M., Lindorff‐Larsen, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.10.653233 · Cited by 5

Harnessing the E3 ligase SPOP for targeted degradation of the NUP98::KDM5A fusion oncoprotein

Kirkiz, E., Kaufmann, G., Bergqvist, S., Fernández‐Pernas, P., Eder, T., Quell, L., Allram, M., Manhart, G., Walter, W., Haferlach, T., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116602 · Cited by 4

CD47 destabilization via manipulating the SPOP-USP2 axis augments macrophage phagocytosis and cancer immunotherapy

Yan, P., Bu, X., Hou, T., Chen, L., Zhong, G., Huang, D., Wang, J., Qi, Y., Jiang, W., Li, Z., et al. (2026) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2025-013498 · Cited by 4

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

Application of A lpha F old models in evaluating ligandable cysteines across E 3 ligases

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Biochemical analysis of PD-L1 ubiquitination by CRL3SPOP, ARIH1, and NEDD4 family ubiquitin ligases

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Regulation of Stem Cells by Cullin-RING Ligase

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Role of conserved Met112 residue in the catalytic activity and stability of ketosteroid isomerase

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SPOP suppresses testicular germ cell tumors progression through ubiquitination and degradation of DPPA2

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Dimerization quality control via ubiquitylation

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LLPSWise - fast and accurate prediction of LLPS constituentsPreprint

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Discovery of 2-Pyrazolylpyrimidinone Derivatives as New SPOP Inhibitors for Renal Cell Carcinoma Therapy

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SPOP mediates apoptosis and protects against necroptosis by regulating ubiquitination of RIPK1 and RIPK3

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Bridged PROTAC, DNA-based PROTAC and hydrophobic tag technologies for targeted protein degradation

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Prevalence of SPOP and IDH Gene Mutations in Prostate Cancer in a Jordanian Population

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The Cullin3-Rbx1-KLHL9 E3 ubiquitin ligase complex ubiquitinates Rheb and supports amino acid-induced mTORC1 activation

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Cul3 substrate adaptor SPOP targets Nup153 for degradation

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C-terminal truncated SPOP, a Janus-faced variant, causing a mixed type 1 and type 2 Nabais Sa-de Vries syndrome

Law, C. Y., & Lam, C. (2022) · Clinica Chimica Acta · doi:10.1016/j.cca.2022.08.019 · Cited by 3

Hidden tricks in MATH: Hypermorphic mutations in SPOP tumor suppressor explained by cryo-EM

Orme, J. J., Mer, G., & Huang, H. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.003 · Cited by 3

Vesicular mechanisms of drug resistance in apicomplexan parasites

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Cancer-associated SPOP mutations enlarge nuclear size and facilitate nuclear envelope rupture upon farnesyltransferase inhibitor treatment

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CRL3-Mediated Ubiquitination in Arabidopsis: Roles of BTB Proteins in Diverse Biological Processes

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Impact of SPOP Mutations on Clinical Outcomes in Metastatic Prostate Cancer

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Molecular insights for the tumor suppressor role of SPOP in prostate cancer

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Nanobody-based bioPROTAC for viral protein degradation provides an antiviral strategy for porcine arterivirus

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1Department of Structural Biology

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Insights into BTB-Cul3 Ubiquitin Ligases from the Structures of SPOP-Substrate Complexes

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Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP

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Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

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