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

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148

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

Jiang, J., & Struhl, G. (1998) · Nature · doi:10.1038/35154 · Cited by 1,735

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

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

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

Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M. G., Harper, J. W., & Elledge, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80098-7 · Cited by 1,421

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

Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,233

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

Mechanism of Cullin3 E3 Ubiquitin Ligase Dimerization

Choo, Y. Y., & Hagen, T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041350 · Cited by 30

SPOP Mutations Target STING1 Signaling in Prostate Cancer and Create Therapeutic Vulnerabilities to PARP Inhibitor–Induced Growth Suppression

Geng, C., Zhang, M.-C., Manyam, G. C., Vykoukal, J. V., Fahrmann, J. F., Peng, S., Wu, C., Park, S., Kondraganti, S., Wang, D., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-1439 · Cited by 33

Genetics and genomics of prostate cancer

Dean, M. C., & Lou, H. (2013) · Asian Journal of Andrology · doi:10.1038/aja.2013.29 · Cited by 29

New strategies to inhibit KEAP1 and the Cul3-based E3 ubiquitin ligases

Canning, P., & Bullock, A. N. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130215 · Cited by 29

Cullin 3 and Its Role in Tumorigenesis

Chen, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_12 · Cited by 29

LncRNA ADAMTS9‐AS2 suppresses the proliferation of gastric cancer cells and the tumorigenicity of cancer stem cells through regulating SPOP

Wang, F., Tang, C., Xu, D., Tang, Y., Jiang, Y., Gao, X., & Xu, J. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15161 · Cited by 29

Targeting Cul3-scaffold E3 ligase complex via KLHL substrate adaptors for cancer therapy

Xiang, S., Shi, X., Chen, P., Chen, Y., Bing, S., Jin, X., Cao, J., Wang, J., Yang, B., Shao, X., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105616 · Cited by 29

Novel insights into the SPOP E3 ubiquitin ligase: From the regulation of molecular mechanisms to tumorigenesis

Li, X.-M., Wu, H., Xia, Q., Zhou, P., Wang, S., Xiao, Y., & Hu, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112882 · Cited by 32

Analysis of dimerization of BTB-IVR domains of Keap1 and its interaction with Cul3, by molecular modeling

Chauhan, N., Chaunsali, L., Deshmukh, P. H., & Padmanabhan, B. (2013) · Bioinformation · doi:10.6026/97320630009450 · Cited by 29

Activity-based profiling of cullin–RING E3 networks by conformation-specific probes

Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., & Schulman, B. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01392-5 · Cited by 31

CRL3IBTK Regulates the Tumor Suppressor Pdcd4 through Ubiquitylation Coupled to Proteasomal Degradation

Pisano, A., Ceglia, S., Palmieri, C., Vecchio, E., Fiume, G., de Laurentiis, A., Mimmi, S., Falcone, C., Iaccino, E., Scialdone, A., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634535 · Cited by 25

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

Hudson, A. M., Mannix, K. M., & Cooley, L. (2015) · Genetics · doi:10.1534/genetics.115.181289 · Cited by 27

The CUL3-SPOP-DAXX axis is a novel regulator of VEGFR2 expression in vascular endothelial cells

Sakaue, T., Sakakibara, I., Uesugi, T., Fujisaki, A., Nakashiro, K., Hamakawa, H., Kubota, E., Joh, T., Imai, Y., Izutani, H., et al. (2017) · Scientific Reports · doi:10.1038/srep42845 · Cited by 30

The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation

Ostertag, M. S., Messias, A. C., Sattler, M., & Popowicz, G. M. (2018) · Structure · doi:10.1016/j.str.2018.10.005 · Cited by 32

SPOP promotes CDCA5 degradation to regulate prostate cancer progression via the AKT pathway

Luo, Z., Wang, J., Zhu, Y., Sun, X., He, C., Cai, M., Ma, J., Wang, Y., & Han, S. (2021) · Neoplasia · doi:10.1016/j.neo.2021.08.002 · Cited by 27

Structural basis for the ubiquitination of G protein βγ subunits by KCTD5/Cullin3 E3 ligase

Jiang, W., Wang, W., Kong, Y., & Zheng, S. (2023) · Science Advances · doi:10.1126/sciadv.adg8369 · Cited by 26

Speckle‐type POZ protein suppresses lipid accumulation and prostate cancer growth by stabilizing fatty acid synthase

Gang, X., Xuan, L., Zhao, X. Y., Lv, Y., Li, F., Wang, Y., & Wang, G. (2019) · The Prostate · doi:10.1002/pros.23793 · Cited by 27

Regulation of Cell Proliferation and Nrf2-Mediated Antioxidant Defense: Conservation of Keap1 Cysteines and Nrf2 Binding Site in the Context of the Evolution of KLHL Family

Shilovsky, G. A., & Dibrova, D. V. (2023) · Life · doi:10.3390/life13041045 · Cited by 27

Dynamic molecular architecture and substrate recruitment of cullin3–RING E3 ligase CRL3KBTBD2

Hu, Y., Zhang, Z., Mao, Q., Zhang, X., Hao, A., Xun, Y., Wang, Y., Han, L., Zhan, W., Liu, Q., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01182-6 · Cited by 26

Advances in KEAP1-based PROTACs as emerging therapeutic modalities: Structural basis and progress

Chen, J., Feng, D., Zhu, R., Li, H., & Chen, L. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103781 · Cited by 29

Ubiquitination-directed cytosolic DNA degradation governs cGAS-STING-mediated immune response to DNA damage

Li, L., Ye, Q., Ma, J., Wang, Z., Liu, T., Lei, Y., Lu, M., Kang, J., Xiang, H., Li, B., et al. (2026) · Cancer Cell · doi:10.1016/j.ccell.2025.12.013 · Cited by 29

The role of cullin proteins in gastric cancer

Chen, P., & Yao, G.-D. (2015) · Tumor Biology · doi:10.1007/s13277-015-4154-z · Cited by 27

Co-adaptor driven assembly of a CUL3 E3 ligase complex

Akopian, D., McGourty, C. A., & Rapé, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.004 · Cited by 26

O-GlcNAcylation of SPOP promotes carcinogenesis in hepatocellular carcinoma

Zhou, P., Chang, W.-Y., Gong, D.-A., Huang, L., Liu, R., Liu, Y., Xia, J. L., Wang, K., Tang, N., & Huang, A. (2023) · Oncogene · doi:10.1038/s41388-022-02589-z · Cited by 26

The Phosphorylation of PDX-1 by Protein Kinase CK2 Is Crucial for Its Stability

Klein, S., Meng, R., Montenarh, M., & Götz, C. (2016) · Pharmaceuticals · doi:10.3390/ph10010002 · Cited by 26

The E3-ome gene-centric compendium reveals the human E3 ligase landscape

Chua, N. K., González-Robles, T. J., Reddington, C. J., Dudley-Fraser, J., Birkinshaw, R. W., Han, J., Solano, A. N., Wong, S. W., Kochańczyk, T., Peter, J. J., et al. (2026) · Cell · doi:10.1016/j.cell.2026.01.029 · Cited by 29

The functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination

Zhai, F., Li, J., Ye, M., & Jin, X. (2022) · Gene · doi:10.1016/j.gene.2022.146562 · Cited by 24

Identification of speckle-type POZ protein somatic mutations in African American prostate cancer

Liu, W., Buckles, E. L., Qian, C., Tadros, A., Majumdar, S., Cvitanovic, J., Zabaleta, J., Estrada, J. J., & Wilson, J. (2014) · Asian Journal of Andrology · doi:10.4103/1008-682x.132470 · Cited by 25

Post-translational modifications of immune checkpoints: unlocking new potentials in cancer immunotherapy

Hu, Q., Shi, Y., Wang, H., Li, B., & Xu, Z. (2025) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00627-6 · Cited by 27

Intracellular Communication among Morphogen Signaling Pathways during Vertebrate Body Plan Formation

Takebayashi‐Suzuki, K., & Suzuki, A. (2020) · Genes · doi:10.3390/genes11030341 · Cited by 24

Intrinsically disordered substrates dictate SPOP subnuclear localization and ubiquitination activity

Usher, E. T., Sabri, N., Rohac, R., Boal, A. K., Mittag, T., & Showalter, S. A. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100693 · Cited by 24

An emerging role for Cullin-3 mediated ubiquitination in sleep and circadian rhythm

Freeman, A. A. H., Mandilaras, K., Missirlis, F., & Sanyal, S. (2013) · Fly · doi:10.4161/fly.23506 · Cited by 24

Hedgehog signaling downregulates Suppressor of Fused through the HIB/SPOP-Crn axis in Drosophila

Liu, C., Zhou, Z., Yao, X., Chen, P., Sun, M., Su, M., Chang, C., Yan, J., Jiang, J., & Zhang, Q. H. (2014) · Cell Research · doi:10.1038/cr.2014.29 · Cited by 25

Structure of the TRAF4 TRAF domain with a coiled-coil domain and its implications for the TRAF4 signalling pathway

Yoon, J. H., Cho, Y., & Park, H. H. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471302333x · Cited by 24

Stability of HIB-Cul3 E3 ligase adaptor HIB Is Regulated by Self-degradation and Availability of Its Substrates

Zhou, Z., Xu, C., Chen, P., Liu, C., Pang, S., Yao, X., & Zhang, Q. H. (2015) · Scientific Reports · doi:10.1038/srep12709 · Cited by 24

The orphan nuclear receptor SHP regulates ER stress response by inhibiting XBP1s degradationPreprint

Sun, S., Kelekar, S., Kliewer, S. A., & Mangelsdorf, D. J. (2019) · Genes & Development · doi:10.1101/gad.326868.119 · Cited by 25

Qing‐Fei‐Pai‐Du decoction and wogonoside exert anti‐inflammatory action through down‐regulating USP14 to promote the degradation of activating transcription factor 2

Xu, X., Xia, J., Zhao, S., Wang, Q., Ge, G., Xu, F., Liu, X., Zhang, W., & Yang, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202100370rr · Cited by 23

Regulation of Hedgehog Signal Transduction by Ubiquitination and Deubiquitination

Zhang, Q., & Jiang, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413338 · Cited by 23

Counting Degrons: Lessons From Multivalent Substrates for Targeted Protein Degradation

Okoye, C. N., Rowling, P. J. E., Itzhaki, L. S., & Lindon, C. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.913063 · Cited by 26

Mechanism of Ψ-Pro/C-degron recognition by the CRL2FEM1B ubiquitin ligase

Chen, X., Raiff, A., Li, S., Guo, Q., Zhang, J., Zhou, H., Timms, R. T., Yao, X., Elledge, S. J., Koren, I., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47890-5 · Cited by 24

Adenovirus Precursor pVII Protein Stability Is Regulated By Its Propeptide Sequence

Inturi, R., Thaduri, S., & Punga, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080617 · Cited by 23

CAND1 exchange factor promotes Keap1 integration into cullin 3-RING ubiquitin ligase during adipogenesis

Dubiel, D., Ordemann, J., Pratschke, J., Dubiel, W., & Naumann, M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.07.013 · Cited by 23

Network Medicine‐Based Strategy Identifies Maprotiline as a Repurposable Drug by Inhibiting PD‐L1 Expression via Targeting SPOP in Cancer

Tian, S., Xu, M., Geng, X., Fang, J., Xu, H., Xue, X., Hu, H., Zhang, Q., Yu, D., Guo, M., et al. (2024) · Advanced Science · doi:10.1002/advs.202410285 · Cited by 22

De Novo Variants in SPOP Cause Two Clinically Distinct Neurodevelopmental Disorders

Sá, M. J. N., Tekle, G. E., de Brouwer, A. P. M., Sawyer, S. L., del Gaudio, D., Parker, M. J., Kanani, F., van den Boogaard, M. H., van Gassen, K. L. I., Allen, M. I. V., et al. (2020) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2020.02.001 · Cited by 23

SPOP and CUL3 Modulate the Sonic Hedgehog Signal Response Through Controlled Degradation of GLI Family Transcription Factors

Umberger, P. A., & Ogden, S. K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.710295 · Cited by 22

SPOP-mutant prostate cancer: Translating fundamental biology into patient care

Bernasocchi, T., & Theurillat, J.-P. P. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.12.024 · Cited by 22

Co-occurring BRCA2/SPOP Mutations Predict Exceptional Poly (ADP-ribose) Polymerase Inhibitor Sensitivity in Metastatic Castration-Resistant Prostate Cancer

Orme, J. J., Taza, F., Sarkar, N. D., Tewari, A. K., Naqvi, S. A. A., Riaz, I. B., Childs, D. S., Omar, N. S., Adra, N., Ashkar, R., et al. (2023) · European Urology Oncology · doi:10.1016/j.euo.2023.11.014 · Cited by 23

Cul3-KLHL20 ubiquitin ligase: physiological functions, stress responses, and disease implications

Chen, H., Liu, C.-C., & Chen, R. (2016) · Cell Division · doi:10.1186/s13008-016-0017-2 · Cited by 21

Identification of a PGXPP degron motif in dishevelled and structural basis for its binding to the E3 ligase KLHL12

Chen, Z., Wasney, G. A., Picaud, S., Filippakopoulos, P., Vedadi, M., D’Angiolella, V., & Bullock, A. N. (2020) · Open Biology · doi:10.1098/rsob.200041 · Cited by 21

Identification of a novel germline SPOP mutation in a family with hereditary prostate cancer

Zuhlke, K. A., Johnson, A., Tomlins, S. A., Palanisamy, N., Carpten, J. D., Lange, E. M., Isaacs, W. B., & Cooney, K. A. (2014) · The Prostate · doi:10.1002/pros.22818 · Cited by 22

Structural Insights into BET Client Recognition of Endometrial and Prostate Cancer-Associated SPOP Mutants

Ostertag, M. S., Hutwelker, W., Plettenburg, O., Sattler, M., & Popowicz, G. M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.017 · Cited by 21

CUL3 and protein kinases: Insights from PLK1/KLHL22 interaction

Metzger, T., Kleiss, C., & Sumara, I. (2013) · Cell Cycle · doi:10.4161/cc.25369 · Cited by 21

Decreased expression of the SPOP gene is associated with poor prognosis in glioma

Ding, D., SONG, T., Wu, J., Tan, Z., & FANG, J. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2729 · Cited by 21

SPOP and FOXA1 mutations are associated with PSA recurrence in ERG wt tumors, and SPOP downregulation with ERG‐rearranged prostate cancer

Hernández‐Llodrà, S., Segalés, L., Safont, A., Juanpere-Rodero, N., Lorenzo, M., Fumadó, L., Rodríguez‐Vida, A., Cecchini, L., Joaquim Bellmunt, B., & Lloreta, J. (2019) · The Prostate · doi:10.1002/pros.23830 · Cited by 21

TGF-β signaling regulates SPOP expression and promotes prostate cancer cell stemness

Jiao, C., Meng, T., Zhou, C., Wang, X., Wang, P., Lü, M., Tan, X., Wei, Q., Ge, X., & Jin, J. (2020) · Aging · doi:10.18632/aging.103085 · Cited by 21

Phosphorylation-dependent regulation of SPOP by LIMK2 promotes castration-resistant prostate cancer

Nikhil, K., Haymour, H. S., Kamra, M., & Shah, K. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01197-6 · Cited by 21

Function, mechanism and drug discovery of ubiquitin and ubiquitin-like modification with multiomics profiling for cancer therapy

Jiang, Y., Ni, S., Xiao, B., & Jia, L. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.07.019 · Cited by 22

SPOP Mutations or ERG Rearrangements Result in Enhanced Levels of ERG to Promote Cell Invasion in Prostate Cancer

Duan, S., & Pagano, M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.003 · Cited by 20

Characterization of Brassica rapa RAP2.4-Related Proteins in Stress Response and as CUL3-Dependent E3 Ligase Substrates

Mooney, S., Al‐Saharin, R., Choi, C. M., Tucker, K., Beathard, C., & Hellmann, H. A. (2019) · Cells · doi:10.3390/cells8040336 · Cited by 20

Androgen Receptor Signaling in Prostate Cancer Genomic Subtypes

Jillson, L. K., Yette, G. A., Laajala, T. D., Tilley, W. D., Costello, J. C., & Cramer, S. D. (2021) · Cancers · doi:10.3390/cancers13133272 · Cited by 20

Intrinsic PD‐L1 Degradation Induced by a Novel Self‐Assembling Hexapeptide for Enhanced Cancer Immunotherapy

Zhang, H., Ji, M. H., Wang, Y., Jiang, M., Lv, Z., Li, G., Wang, L., & Zheng, Z. (2024) · Advanced Science · doi:10.1002/advs.202410145 · Cited by 19

SPOP targets the immune transcription factor IRF1 for proteasomal degradation

Schwartz, I., Vunjak, M., Budroni, V., Garcia, A. C., Mastrovito, M., Söderholm, A., Hinterndorfer, M., de Almeida, M., Hacker, K., Wang, J., et al. (2023) · eLife · doi:10.7554/elife.89951 · Cited by 18

Molecular basis for C-degron recognition by CRL2 APPBP2 ubiquitin ligase

Zhao, S., Olmayev-Yaakobov, D., Ru, W., Li, S., Chen, X., Zhang, J., Yao, X., Koren, I., Zhang, K., & Xu, C. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2308870120 · Cited by 17

Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex

Horn‐Ghetko, D., Hopf, L. V. M., Tripathi‐Giesgen, I., Du, J., Kostrhon, S., Vu, D. T., Beier, V., Steigenberger, B. A., Prabu, J. R., Stier, L. J., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01257-y · Cited by 18

JMJD6 Rewires ATF4-Dependent Glutathione Metabolism to Confer Ferroptosis Resistance in SPOP-Mutated Prostate Cancer

Zhang, C., Ding, J., Lim, K. S., Zhou, W., Miao, W., Wu, S., Liu, H., Huang, D., Chen, C., He, H., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-23-2796 · Cited by 18

Negative Regulation of the Innate Immune Response through Proteasomal Degradation and Deubiquitination

Budroni, V., & Versteeg, G. A. (2021) · Viruses · doi:10.3390/v13040584 · Cited by 21

PUP-IT2 as an alternative strategy for PUP-IT proximity labeling

Yue, S., Xu, P. H., Cao, Z., & Zhuang, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1007720 · Cited by 18

Molecular evolution of Keap1 was essential for adaptation of vertebrates to terrestrial life

Yumimoto, K., Sugiyama, S., Motomura, S., Takahashi, D., & Nakayama, K. I. (2023) · Science Advances · doi:10.1126/sciadv.adg2379 · Cited by 19

Identification and Expression Profiling of the BTB Domain-Containing Protein Gene Family in the Silkworm,Bombyx mori

Cheng, D., Qian, W., Meng, M., Wang, Y., Peng, J., & Xia, Q. (2014) · International Journal of Genomics · doi:10.1155/2014/865065 · Cited by 19

The Roles of SPOP in DNA Damage Response and DNA Replication

Maekawa, M., & Higashiyama, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197293 · Cited by 18

Molecular Interplay between AURKA and SPOP Dictates CRPC Pathogenesis via Androgen Receptor

Nikhil, K., Kamra, M., Raza, A., Haymour, H. S., & Shah, K. (2020) · Cancers · doi:10.3390/cancers12113247 · Cited by 18

Cul3-KLHL20 E3 ubiquitin ligase plays a key role in the arms race between HIV-1 Nef and host SERINC5 restriction

Li, S., Li, R., Ahmad, I., Liu, X., Johnson, S. F., Sun, L., & Zheng, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-30026-y · Cited by 18

Molecular basis of cullin-3 (Cul3) ubiquitin ligase subversion by vaccinia virus protein A55

Gao, C., Pallett, M. A., Croll, T. I., Smith, G. L., & Graham, S. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006561 · Cited by 17

Substrate-dependent interaction of SPOP and RACK1 aggravates cardiac fibrosis following myocardial infarction

Yang, W., Zhuang, Y., Wu, H., Su, S., Li, Y., Wang, C., Tian, Z., Peng, L.-L., Zhang, X., Liu, J., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.015 · Cited by 17

Skraban‐Deardorff intellectual disability syndrome‐associated mutations in WDR 26 impair CTLH E 3 complex assembly

Groß, A., Müller, J., Chrustowicz, J., Strasser, A., Gottemukkala, K. V., Sherpa, D., Schulman, B. A., Murray, P. J., & Alpi, A. F. (2024) · FEBS Letters · doi:10.1002/1873-3468.14866 · Cited by 17

A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3KLHL22

Wang, W., Liang, L., Dai, Z., Zuo, P., Yu, S., Lu, Y., Ding, D., Chen, H., Shan, H., Jin, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48045-2 · Cited by 17

Transfer of Ho Endonuclease and Ufo1 to the Proteasome by the UbL-UbA Shuttle Protein, Ddi1, Analysed by Complex Formation In Vitro

Voloshin, O., Bakhrat, A., Herrmann, S., & Raveh, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039210 · Cited by 17

Viral Manipulations of the Cullin-RING Ubiquitin Ligases

Liu, Y., & Tan, X. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_7 · Cited by 17

Harnessing the SPOP E3 Ubiquitin Ligase via a Bridged Proteolysis Targeting Chimera (PROTAC) Strategy for Targeted Protein Degradation

Deng, Z., Catlett, J. L., Lee, Y., Wu, Q. D., Xu, Z., Xie, L., Chen, X., Xiong, Y., Kanıskan, H. Ü., & Jin, J. J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00295 · Cited by 18

Biophysical insights into glucose-dependent transcriptional regulation by PDX1

Usher, E. T., & Showalter, S. A. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102623 · Cited by 17

SPOP in Cancer: Phenomena, Mechanisms and Its Role in Therapeutic Implications

Yang, X., & Zhu, Q. (2022) · Genes · doi:10.3390/genes13112051 · Cited by 16

Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme

Teng, F., Wang, Y., Liu, M., Tian, S., Stjepanović, G., & Su, M.-Y. (2023) · Structure · doi:10.1016/j.str.2023.09.002 · Cited by 16

N6-methyladenosine modification of SPOP relieves ferroptosis and diabetic cardiomyopathy by enhancing ubiquitination of VDAC3

Meng, W., & Li, L. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.025 · Cited by 16

SCF Cdc4 Enables Mating Type Switching in Yeast by Cyclin-Dependent Kinase-Mediated Elimination of the Ash1 Transcriptional Repressor

Liu, Q., Larsen, B. G., Řičicová, M., Orlicky, S. M., Tekotte, H., Tang, X., Craig, K. L., Quiring, A., Bihan, T. L., Hansen, C. L., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00845-10 · Cited by 17

KLHL6 is a tumor suppressor gene in diffuse large B-cell lymphoma

Choi, J., Zhou, N., & Busino, L. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1568765 · Cited by 18

Human Histone Interaction Networks: An Old Concept, New Trends

Peng, Y., Markov, Y., Goncearenco, A., Landsman, D., & Panchenko, A. R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.10.018 · Cited by 16

RNA interference-mediated silencing of speckle-type POZ protein promotes apoptosis of renal cell cancer cells

Sun, G.-L., Liu, X., & Sun, X. (2016) · OncoTargets and Therapy · doi:10.2147/ott.s91097 · Cited by 16

SPOP Targets Oncogenic Protein ZBTB3 for Destruction to Suppress Endometrial CancerPreprint

Jin, X., Wang, J., Li, Q., Zhuang, H., Yang, J., Lin, Z.-H., Lin, T., Lv, Z., Shen, L., Yan, C., et al. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3491871 · Cited by 16

Bivalent target-binding bioPROTACs induce potent degradation of oncogenic SHP2

Hoffman, M., Krum, D., & Wittrup, K. D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107616 · Cited by 16

A phospho-tyrosine–based signaling module using SPOP, CSK, and LYN controls TLR-induced IRF activity

Tawaratsumida, K., Redecke, V., Wu, R., Kuriakose, J. A., Bouchard, J. J., Mittag, T., Lohman, B. K., Mishra, A., High, A. A., & Häcker, H. (2022) · Science Advances · doi:10.1126/sciadv.abq0084 · Cited by 17

Functional roles of E3 ubiquitin ligases in prostate cancer

Zhao, Y., Li, J., Chen, J., Ye, M., & Jin, X. (2022) · Journal of Molecular Medicine · doi:10.1007/s00109-022-02229-9 · Cited by 15

SPOP loss of function protects against tauopathy

Eck, R. J., Kow, R. L., Black, A. H., Liachko, N. F., & Kraemer, B. C. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207250120 · Cited by 16

Molecular features and race‐associated outcomes of SPOP ‐mutant metastatic castration‐resistant prostate cancer

Stangl, A., Wilner, C., Li, P., Maahs, L., Hwang, C., & Pilling, A. B. (2023) · The Prostate · doi:10.1002/pros.24481 · Cited by 15

SPOP point mutations regulate substrate preference and affect its function

Deng, Y., Ding, W., Ma, K., Zhan, M., Sun, L., Zhou, Z., & Lu, L. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06565-1 · Cited by 15

Targeting kelch-like (KLHL) proteins: achievements, challenges and perspectives

Zhou, Y., Zhang, Q., Zhao, Z., Hu, X., You, Q., & Jiang, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116270 · Cited by 15

Speckle-type POZ protein functions as a tumor suppressor in non-small cell lung cancer due to DNA methylation

Yao, S., Chen, X., Chen, J., Guan, Y., Liu, Y., Chen, J., & Lv, X. (2018) · Cancer Cell International · doi:10.1186/s12935-018-0711-z · Cited by 15

Spop ameliorates diabetic nephropathy through restraining NLRP3 inflammasome

Wang, B., Dai, Z.-H., Gao, Q., Liu, Y., Gu, G., & Zheng, H. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.12.068 · Cited by 15

Phylogenetic Analysis of Brassica rapa MATH-Domain Proteins

Zhao, L., Huang, Y., Hu, Y., He, X., Shen, W., Liu, C., & Ruan, Y. (2013) · Current Genomics · doi:10.2174/1389202911314030007 · Cited by 15

Solution Ensemble of the C-Terminal Domain from the Transcription Factor Pdx1 Resembles an Excluded Volume Polymer

Cook, E. C., Sahu, D., Bastidas, M., & Showalter, S. A. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b10051 · Cited by 15

In-Cell Approach to Evaluate E3 Ligases for Use in Targeted Protein Degradation

Zheng, Y., Singh, A., Niu, Z., Marin, V. L., Young, J., Richardson, P. L., Hemshorn, M. L., Cooley, R. B., Karplus, P. A., Puvar, K., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c02741 · Cited by 16

1Department of Structural Biology

Ligases, O. B.-C. U., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., Hoggard, T., Harper, J. W., White, K. P., & Schulman, B. A. (2015)

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

Zhuang, M. (2009) · doi:10.21007/etd.cghs.2009.0386

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

van Geersdaele, L. K., Stead, M., Harrison, C. M., Carr, S. B., Close, H. J., Rosbrook, G. O., Connell, S. D., & Wright, S. C. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913012687 · Cited by 40

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

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284

BTB proteins as henchmen of Cul3-based ubiquitin ligases

Krek, W. (2003) · Nature Cell Biology · doi:10.1038/ncb1103-950 · Cited by 65