Structural assembly of cullin-RING ubiquitin ligase complexes

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840

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

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184

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

Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224

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

Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants

Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947

SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27

Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544

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

Multimeric Complexes among Ankyrin-Repeat and SOCS-box Protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the Structure and Assembly of ECS-type Cullin-RING E3 Ubiquitin Ligases

Thomas, J. C., Matak‐Vinković, D., Molle, I. V., & Ciulli, A. (2013) · Biochemistry · doi:10.1021/bi400758h · Cited by 33

Biophysical Studies on Interactions and Assembly of Full-size E3 Ubiquitin Ligase

Bulatov, E., Martin, E. M., Chatterjee, S., Knebel, A., Shimamura, S., Konijnenberg, A., Johnson, C., Zinn, N., Grandi, P., Sobott, F., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616664 · Cited by 30

O2 sensing–associated glycosylation exposes the F-box–combining site of the Dictyostelium Skp1 subunit in E3 ubiquitin ligases

Sheikh, M. O., Thieker, D. F., Chalmers, G., Schafer, C. M., Ishihara, M., Azadi, P., Woods, R. J., Glushka, J., Bendiak, B. K., Prestegard, J. H., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809160 · 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

Loss of DDB1 Leads to Transcriptional p53 Pathway Activation in Proliferating Cells, Cell Cycle Deregulation, and Apoptosis in Zebrafish Embryos

Hu, Z., Holzschuh, J., & Driever, W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134299 · Cited by 31

Secondary interactions involving zinc-bound ligands: Roles in structural stabilization and macromolecular interactions

Namuswe, F., & Berg, J. M. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.10.018 · Cited by 32

Targeting the E3 ubiquitin ligases DCAF15 and cereblon for cancer therapy

Nguyen, K. M., & Busino, L. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.03.007 · Cited by 29

The application of ubiquitin ligases in the PROTAC drug design

Chen, Y., & Jin, J. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa053 · Cited by 29

Glycosylation of Skp1 Affects Its Conformation and Promotes Binding to a Model F-Box Protein

Sheikh, M. O., Schafer, C. M., Powell, J. T., Rodgers, K. K., Mooers, B. H. M., & West, C. M. (2014) · Biochemistry · doi:10.1021/bi401707y · Cited by 26

Nuclear and cytoplasmic WDR-23 isoforms mediate differential effects on GEN-1 and SKN-1 substrates

Spatola, B. N., Lo, J. Y., Wang, B., & Curran, S. P. (2019) · Scientific Reports · doi:10.1038/s41598-019-48286-y · Cited by 25

The BTB/POZ domain protein GmBTB/POZ promotes the ubiquitination and degradation of the soybean AP2/ERF-like transcription factor GmAP2 to regulate the defense response to Phytophthora sojae

Zhang, C., Gao, H., Sun, Y., Jiang, L., He, S., Song, B., Liu, S., Zhao, M., Wang, L., Liu, Y., et al. (2021) · Journal of Experimental Botany · doi:10.1093/jxb/erab363 · Cited by 27

CUL3/SPOP complex prevents immune escape and enhances chemotherapy sensitivity of ovarian cancer cells through degradation of PD-L1 protein

Dong, M., Qian, M., & Ruan, Z. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-005270 · Cited by 28

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

Flipping the Switch from G1 to S Phase with E3 Ubiquitin Ligases

Rizzardi, L. F., & Cook, J. G. (2012) · Genes & Cancer · doi:10.1177/1947601912473307 · Cited by 27

Breaking Bad Proteins—Discovery Approaches and the Road to Clinic for Degraders

Bouvier, C., Lawrence, R., Cavallo, F., Xolalpa, W., Jordan, A. M., Hjerpe, R., & Rodríguez, M. S. (2024) · Cells · doi:10.3390/cells13070578 · Cited by 28

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

Cul4-Ddb1 ubiquitin ligases facilitate DNA replication-coupled sister chromatid cohesion through regulation of cohesin acetyltransferase Esco2

Sun, H., Zhang, J., Xin, S., Jiang, M., Zhang, J., Li, Z., Cao, Q., & Lou, H. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1007685 · Cited by 27

Role of the COP9 Signalosome (CSN) in Cardiovascular Diseases

Milic, J., Tian, Y., & Bernhagen, J. (2019) · Biomolecules · doi:10.3390/biom9060217 · Cited by 27

Towards a Molecular Understanding of the Fanconi Anemia Core Complex

Hodson, C., & Walden, H. (2012) · Anemia · doi:10.1155/2012/926787 · Cited by 27

Cullin 7 mediates proteasomal and lysosomal degradations of rat Eag1 potassium channels

Hsu, P., Ma, Y.-T., Fang, Y.-C., Huang, J.-J., Gan, Y., Chang, P.-T., Jow, G., Tang, C., & Jeng, C. (2017) · Scientific Reports · doi:10.1038/srep40825 · Cited by 26

CUL4-DDB1-CRBN E3 Ubiquitin Ligase Regulates Proteostasis of ClC-2 Chloride Channels: Implication for Aldosteronism and Leukodystrophy

Fu, S.-J., Hu, M., Peng, Y.-J., Fang, H.-Y., Hsiao, C.-T., Chen, T., Jeng, C., & Tang, C. (2020) · Cells · doi:10.3390/cells9061332 · Cited by 25

UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

Hellerschmied, D., Roessler, M., Lehner, A., Gazda, L., Stejskal, K., Imre, R., Mechtler, K., Dammermann, A., & Clausen, T. (2018) · Nature Communications · doi:10.1038/s41467-018-02924-7 · Cited by 25

CRBN‐PROTACs in Cancer Therapy: From Mechanistic Insights to Clinical Applications

Thapa, R., Bhat, A. A., Gupta, G., Jyothi, S. R., Kaur, I., Kumar, S., Sharma, N., Prasad, G. V. S., Pramanik, A., & Ali, H. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70009 · Cited by 26

Identification of Respiratory Syncytial Virus Nonstructural Protein 2 Residues Essential for Exploitation of the Host Ubiquitin System and Inhibition of Innate Immune Responses

Whelan, J. N., Tran, K. C., van Rossum, D. B., & Teng, M. N. (2016) · Journal of Virology · doi:10.1128/jvi.00423-16 · Cited by 24

The crystal structure of the Sgt1-Skp1 complex: the link between Hsp90 and both SCF E3 ubiquitin ligases and kinetochores

Willhöft, O., Kerr, R., Patel, D., Zhang, W., Al-Jassar, C., Daviter, T., Millson, S. H., Thalassinos, K., & Vaughan, C. K. (2017) · Scientific Reports · doi:10.1038/srep41626 · Cited by 24

Fbxo28 promotes mitotic progression and regulates topoisomerase IIα-dependent DNA decatenation

Kratz, A.-S., Richter, K. T., Schlosser, Y. T., Schmitt, M., Shumilov, A., Delecluse, H., & Hoffmann, I. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1246093 · Cited by 23

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

Arabidopsis CRL4 Complexes: Surveying Chromatin States and Gene Expression

Fonseca, S., & Rubio, V. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01095 · Cited by 21

Structure of the DDB1-AMBRA1 E3 ligase receptor complex linked to cell cycle regulation

Liu, M., Wang, Y., Teng, F., Mai, X., Wang, X., Su, M.-Y., & Stjepanović, G. (2023) · Nature Communications · doi:10.1038/s41467-023-43174-6 · Cited by 21

Development of novel benzimidazole-derived neddylation inhibitors for suppressing tumor growth in vitro and in vivo

Chen, X., Yang, X., Mao, F., Wei, J., Xu, Y., Li, B., Zhu, J., Ni, S., Jia, L., & Li, J. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112964 · Cited by 21

Characterization of a cytoplasmic glucosyltransferase that extends the core trisaccharide of the Toxoplasma Skp1 E3 ubiquitin ligase subunit

Rahman, K., Mandalasi, M., Zhao, P., Sheikh, M. O., Taujale, R., Kim, H. W., van der Wel, H., Matta, K. L., Kannan, N., Glushka, J., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809301 · Cited by 20

Proteostasis impairment and ALS

Lambert-Smith, I. A., Saunders, D. N., & Yerbury, J. J. (2022) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2022.06.001 · Cited by 19

CRL2APPBP2-mediated TSPYL2 degradation counteracts human mesenchymal stem cell senescence

Huang, D., Zhao, Q., Yang, K., Lei, J., Jing, Y., Li, H., Zhang, C., Ma, S., Sun, S., Cai, Y., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2451-3 · Cited by 20

DCNL1 Functions as a Substrate Sensor and Activator of Cullin 2-RING Ligase

Heir, P., Sufan, R. I., Greer, S. N., Poon, B., Lee, J. E., & Ohh, M. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01342-12 · Cited by 23

Nucleocytoplasmic O-glycosylation in protists

West, C. M., & Kim, H. W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.031 · Cited by 19

Cullin-RING Ligase Regulation by the COP9 Signalosome: Structural Mechanisms and New Physiologic Players

Rao, F., Lin, H., & Su, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_4 · Cited by 19

Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses

Banchenko, S., Krupp, F., Gotthold, C., Bürger, J., Graziadei, A., O’Reilly, F. J., Sinn, L. R., Ruda, O., Rappsilber, J., Spahn, C. M. T., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009775 · Cited by 17

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

Structural insights into the ubiquitylation strategy of the oligomeric CRL2FEM1B E3 ubiquitin ligase

Dai, Z., Liang, L., Wang, W., Zuo, P., Yu, S. J., Liu, Y., Zhao, X., Lu, Y., Jin, Y., Zhang, F., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00047-y · Cited by 18

Regulation of Unperturbed DNA Replication by Ubiquitylation

Moreno, S. P., & Gambus, A. (2015) · Genes · doi:10.3390/genes6030451 · Cited by 19

CRL7SMU1 E3 ligase complex-driven H2B ubiquitylation functions in sister chromatid cohesion by regulating SMC1 expression

Shah, V. J., & Maddika, S. (2018) · Journal of Cell Science · doi:10.1242/jcs.213868 · Cited by 18

Coexistence of schwannomatosis and glioblastoma in two families

Deiller, C., Van‐Gils, J., Zordan, C., Tinat, J., Loiseau, H., Fabre, T., Delleci, C., Cohen, J., Vidaud, M., Parfait, B., et al. (2019) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2019.103680 · Cited by 17

Association of mRNA expression levels of Cullin family members with prognosis in breast cancer

Liu, A., Zhang, S., Shen, Y., Lei, R., & Wang, Y. (2019) · Medicine · doi:10.1097/md.0000000000016625 · Cited by 17

High Expression of Cullin7 Correlates with Unfavorable Prognosis in Epithelial Ovarian Cancer Patients

Xi, J., Zeng, S., Guo, L., & Feng, J. C. (2016) · Cancer Investigation · doi:10.3109/07357907.2015.1114123 · Cited by 16

Glycosylation Promotes the Random Coil to Helix Transition in a Region of a Protist Skp1 Associated with F-Box Binding

Xu, X. M., Eletsky, A., Sheikh, M. O., Prestegard, J. H., & West, C. M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01033 · Cited by 16

Novel KLHL26 variant associated with a familial case of Ebstein’s anomaly and left ventricular noncompaction

Thareja, S. K., North, L. M., Stamm, K., Earing, M. G., Frommelt, M. A., Willes, R. J., Tripathi, S., Dsouza, N. R., Zimmermann, M. T., Mahnke, D. K., et al. (2020) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.1152 · Cited by 16

Skp1 Dimerization Conceals Its F-Box Protein Binding Site

Kim, H. W., Eletsky, A., Gonzalez, K. J., van der Wel, H., Strauch, E., Prestegard, J. H., & West, C. M. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00094 · Cited by 16

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

Structural basis for Cullins and RING component inhibition: Targeting E3 ubiquitin pathway conductors for cancer therapeutics

Shafique, S., Ali, W., Kanwal, S., & Rashid, S. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.08.047 · Cited by 16

Entropy-Driven Mechanism of an E3 Ligase

Truong, K., Su, Y., Song, J., & Chen, Y. (2011) · Biochemistry · doi:10.1021/bi2001856 · Cited by 14

Function and regulation of F‑box/WD repeat‑containing protein 7 (Review)

Zhang, Z., Hu, Q., Xu, W., Liu, W., Liu, M., Sun, Q., Zeng, Y., Fan, G., Qin, Y., Xu, X., et al. (2020) · Oncology Letters · doi:10.3892/ol.2020.11728 · 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

Genome-wide identification, sequence characterization, and protein–protein interaction properties of DDB1 (damaged DNA binding protein-1)-binding WD40-repeat family members in Solanum lycopersicum

Zhu, Y., Huang, S., Miao, M., Tang, X., Yue, J., Wang, W., & Liu, Y. (2015) · Planta · doi:10.1007/s00425-015-2258-8 · Cited by 14

How the Ankyrin and SOCS Box Protein, ASB9, Binds to Creatine Kinase

Balasubramaniam, D., Schiffer, J. M., Parnell, J., Mir, S. P., Amaro, R. E., & Komives, E. A. (2015) · Biochemistry · doi:10.1021/bi501420n · Cited by 15

SKP1-like protein, CrSKP1-e, interacts with pollen-specific F-box proteins and assembles into SCF-type E3 complex in ‘Wuzishatangju’ (Citrus reticulata Blanco) pollen

Ren, Y., Hua, Q., Pan, J., Zhang, Z., Zhao, J., He, X., Qin, Y., & Hu, G. (2020) · PeerJ · doi:10.7717/peerj.10578 · Cited by 13

Crt10 directs the cullin-E3 ligase Rtt101 to nonfunctional 25S rRNA decay

Sakata, T., Fujii, K., Ohno, M., & Kitabatake, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.072 · Cited by 12

The Cullin-4 Complex DCDC Does Not Require E3 Ubiquitin Ligase Elements To Control Heterochromatin in Neurospora crassa

Adhvaryu, K. K., Gessaman, J. D., Honda, S., Lewis, Z., Grisafi, P. L., & Selker, E. U. (2014) · Eukaryotic Cell · doi:10.1128/ec.00212-14 · Cited by 12

Dbo/Henji Modulates Synaptic dPAK to Gate Glutamate Receptor Abundance and Postsynaptic Response

Wang, M., Chen, P., Wang, C.-H., Lai, T.-T., Tsai, P.-I., Cheng, Y.-J., Kao, H.-H., & Chien, C. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006362 · Cited by 10

Control of Genome through Variative Nature of Histone-Modifying Ubiquitin Ligases

Bacheva, A. V., Gotmanova, N. N., Belogurov, A. A., & Kudriaeva, A. A. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921140066 · Cited by 11

NAE modulators: A potential therapy for gastric carcinoma

Liang, Q., Liu, M., Li, J. H., Tong, R., Hu, Y., Bai, L., & Shi, J. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114156 · Cited by 11

The Cellular and Developmental Roles of Cullins, Neddylation, and the COP9 Signalosome in Dictyostelium discoideum

Kim, W. D., Mathavarajah, S., & Huber, R. J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.827435 · Cited by 11

Non-Canonical CRL4A/4BCDT2 Interacts with RAD18 to Modulate Post Replication Repair and Cell Survival

Sertic, S., Evolvi, C., Tumini, E., Plevani, P., Muzi-Falconi, M., & Rotondo, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060000 · Cited by 12

Insights in cullin 3/WNK4 and its relationship to blood pressure regulation and electrolyte homeostasis

Andérica‐Romero, A. C., Escobar, L. I., Padilla‐Flores, T., & Pedraza‐Chaverrí, J. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.01.032 · Cited by 12

Structural mechanism of CRL4‐instructed STAT2 degradation via a novel cytomegaloviral DCAF receptor

Le‐Trilling, V. T. K., Banchenko, S., Paydar, D., Leipe, P. M., Binting, L., Lauer, S., Graziadei, A., Klingen, R., Gotthold, C., Bürger, J., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112351 · Cited by 10

From serendipity to strategy: molecular glue degraders in cancer therapeutics

Darling, S., Bajrami, I., & West, S. C. (2025) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2025.2564068 · Cited by 9

Binding to DCAF1 distinguishes TASOR and SAMHD1 degradation by HIV-2 Vpx

Martin, M. M., Matkovic, R., Larrous, P., Morel, M., Lasserre, A., Vauthier, V., & Margottin-Goguet, F. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009609 · Cited by 14

Drosophila Cul3 contributes to Diap2-mediated innate immune signaling for antimicrobial defense

Kong, F., Wang, Z., Zhang, C., Xiao, Y., Saeed, M. A. R., Li, W., Goto, A., Cai, Q., & Ji, S. (2024) · hLife · doi:10.1016/j.hlife.2024.10.001 · Cited by 9

Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis

Mathur, R., Yen, J. L., & Kaiser, P. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005727 · Cited by 9

Heat shock protein 60 negatively regulates the biological functions of ubiquitin-like protein MNSFβ in macrophages

Nakamura, M., Notsu, K., & Nakagawa, M. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-018-3487-5 · Cited by 9

Cullin7 in tumor development: a novel potential anti-cancer target

Li, Y., Zang, A., Fu, J., & Jia, Y. (2021) · Neoplasma · doi:10.4149/neo_2021_201207n1324 · Cited by 8

Biochemical strategies of E3 ubiquitin ligases target viruses in critical diseases

Dubey, A. R., Jagtap, Y. A., Kumar, P., Patwa, S. M., Kinger, S., Kumar, A., Singh, S., Prasad, A., Jana, N. R., & Mishra, A. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30143 · Cited by 8

Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation

Dohmen, R. J., Huibregtse, J. M., & Scheffner, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10069-0 · Cited by 8

Ringside views

Malim, M. H. (2014) · Nature · doi:10.1038/505167a · 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

Unlocking DCAFs To Catalyze Degrader Development: An Arena for Innovative Approaches

Miao, Q., Kadam, V. D., Mukherjee, A., Tan, Z., & Teng, M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01209 · Cited by 7

Interplay between NRF2 post-translational modifications and protein-protein interactions: Perspectives from emerging structural and functional evidence

Ozleyen, A., Kulabas, S. S., Novak, M. J., Cichoń, M., Heras, C. M. D. L., Honda, T., Doveston, R. G., Dinkova‐Kostova, A. T., Grochot‐Przeczek, A., & Tumer, T. B. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110847 · Cited by 5

Probing the CRL4DCAF12 interactions with MAGEA3 and CCT5 di-Glu C-terminal degrons

Righetto, G. L., Yin, Y., Duda, D. M., Vu, V., Szewczyk, M. M., Zeng, H., Li, Y., Loppnau, P., Mei, T., Li, Y.-Y., et al. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae153 · Cited by 5

Molecular insights into degron recognition by CRL5ASB7 ubiquitin ligase

Zhou, M., Wang, X., Li, J., Ma, J., Bao, Z., Yan, X., Zhang, B., Liu, T., Yu, Y., Mi, W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50556-x · Cited by 5

CAND1 inhibits Cullin-2-RING ubiquitin ligases for enhanced substrate specificity

Wang, K., Diaz, S., Li, L., Lohman, J. R., & Liu, X. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01167-5 · Cited by 5

Hepatic WDR23 proteostasis mediates insulin homeostasis by regulating insulin-degrading enzyme capacity

Duangjan, C., Arpawong, T. E., Spatola, B. N., & Curran, S. P. (2024) · GeroScience · doi:10.1007/s11357-024-01196-y · Cited by 4

Comprehensive analysis of the Cullin family of genes reveals that CUL7 and CUL9 are the significant prognostic biomarkers in colorectal cancer

Zhang, L. (2024) · American Journal of Translational Research · doi:10.62347/chib8915 · Cited by 4

Illuminating ubiquitination mechanisms: How cryo-EM has shed light on Cullin RING E3 ligase function

Rizvi, Z., & Lander, G. C. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103055 · Cited by 5

Aldosterone defects in infants and young children with hyperkalemia: A single center retrospective study

Liu, X., Xie, Y., Tang, J., Zhong, J., Zeng, D. L., & Lan, D. (2023) · Frontiers in Pediatrics · doi:10.3389/fped.2023.1092388 · Cited by 3

Overview of Protein Degradation in Plant Hormone Signaling

Rusnac, D. V., & Zheng, N. (2018) · Springer eBooks · doi:10.1007/978-3-319-91352-0_2 · Cited by 3

Cul2 Is Essential for the Drosophila IMD Signaling-Mediated Antimicrobial Immune Defense

Duan, R., Hu, B., Ding, E., Zhang, S., Wu, M., Jin, Y., Ali, U., Saeed, M. A. R., Raza, B., Usama, M., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062627 · Cited by 3

Physiology and Pathophysiology of the NaCl Co-Transporters in the Kidney

Gamba, G. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381462-3.00032-x · Cited by 3

Inhibiting Neddylation with MLN4924 Suppresses Growth and Delays Multicellular Development in Dictyostelium discoideum

Huber, R. J., Kim, W. D., & Mathavarajah, S. (2021) · Biomolecules · doi:10.3390/biom11030482 · Cited by 3

Familial Hyperkalemic Hypertension (FHHt)

Rafael, C., & Hadchouel, J. (2023) · Endocrinology · doi:10.1007/978-3-031-27119-9_4 · Cited by 2

CRL4 mediates autoubiquitination of DDB1 upon deneddylation inhibition

Kim, Y.-M., Jo, J.-H., Kim, D., Park, J.-U., Jung, D.-H., Cho, H. J., Seong, H., Nah, J., Park, J.-Y., Choi, J.-H., et al. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152772 · Cited by 2

A dual system to manipulate protein levels for DNA replication- and cell cycle-related studies

García‐Rodríguez, N., & Ulrich, H. D. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.038 · Cited by 2

The differentially expressed gene signatures of the Cullin 3-RING ubiquitin ligases in neuroendocrine cancer

Park, J.-U., Kim, D.-K., Kim, J., Jo, J.-H., Kim, Y.-M., Jung, D.-H., Kim, H., Ok, S.-M., Cho, H. J., Kim, S., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.10.108 · Cited by 2

KCTD Family: Emerging Regulators of GPCR Biased Signaling

Jiang, W., & Zheng, S. (2025) · Handbook of experimental pharmacology · doi:10.1007/164_2025_766 · Cited by 1

Regulation of PD-L1 Protein Expression by the E3 Ubiquitin Ligase GP78

Chatterjee, M., Pimentel, J. M., Zhou, J., Mugunamalwaththa, T., Yang, Z., Raz, A., & Wu, G. S. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47100829 · Cited by 1

Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1

Andree, G. A., Stier, L. J., Schmiederer, K., Thielen, A. S., Schmid, L., Maiwald, S. A., Gottemukkala, K. V., Du, J., von Gronau, S., Strasser, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72524-3 · Cited by 1

Crystal structure of MutYX: a novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-oxoguanine recognition sphere

Trasviña‐Arenas, C. H., Hashemian, M., Malek, M., Merrill, S., Fisher, A. J., & David, S. S. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1127 · Cited by 1

Structures of ZYG11B-EloB-EloC-substrate complex reveal mechanisms of CRL2ZYG11B assembly and function

Lin, N., Feng, H., Geng, Y., Gao, Y., Shi, M., Liu, S., Gao, P., & Wang, Y. (2026) · Nature Communications · doi:10.1038/s41467-026-71318-x · Cited by 1

The Crossroads of Ubiquitination and DNA Repair: A Structural Perspective

Lingaraju, G. M., Böhm, K., Rabl, J., Cavadini, S., Fischer, E. S., Kassube, S. A., & Thomä, N. H. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_9 · Cited by 1

A useful toolbox for the detection of SCF E3 ligase activity

Casagrande, F., Xie, Q., & Serino, G. (2022) · Molecular Plant · doi:10.1016/j.molp.2022.09.022 · Cited by 1

Structural Insight Into the SKP1 ‐ CUL1 ‐ FBXO3 ‐ RBX1 Complex

Wei, J., & Xu, C. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26809 · Cited by 1

Hepatic WDR23 proteostasis mediates insulin clearance by regulating insulin-degrading enzymePreprint

Duangjan, C., Arpawong, T. E., Spatola, B. N., & Curran, S. P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.24.516014 · Cited by 1

Structural Biology of CRL Ubiquitin Ligases

Rusnac, D.-V., & Zheng, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_2 · Cited by 53

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction

Nguyen, H. C., Wang, W., & Xiong, Y. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-46503-6_12 · Cited by 102

Aufklärung der Strukturen und Mechanismen von großen nicht-kanonischen Cullin-RING-Ligasen

Hopf, L. V. M. (2025) · mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich)

The Dynamic Self-regulation of Modular Cullin-Ring Ligases

Lumpkin, R. J., & Komives, E. A. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.2266

Elucidating structures and mechanisms of large non-canonical cullin-RING ligases

Hopf, L. V. M., Schulman, B. A., & München, T. U. (2024)