Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome

The DNA Damage Response: Making It Safe to Play with Knives

Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368

Identification of a Primary Target of Thalidomide Teratogenicity

Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Yamaguchi, Y., & Handa, H. (2010) · Science · doi:10.1126/science.1177319 · Cited by 2,136

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

Lenalidomide Causes Selective Degradation of IKZF1 and IKZF3 in Multiple Myeloma Cells

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Quantifying the local resolution of cryo-EM density maps

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The Myeloma Drug Lenalidomide Promotes the Cereblon-Dependent Destruction of Ikaros Proteins

Lu, G., Middleton, R. E., Sun, H., Naniong, M., Ott, C. J., Mitsiades, C. S., Wong, K.-K., Bradner, J. E., & Kaelin, W. G. (2014) · Science · doi:10.1126/science.1244917 · Cited by 1,583

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

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ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures

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Understanding nucleotide excision repair and its roles in cancer and ageing

Marteijn, J. A., Lans, H., Vermeulen, W., & Hoeijmakers, J. H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3822 · Cited by 1,192

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

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Targeting the COP9 signalosome for cancer therapy

Du, W., Zhang, R., Muhammad, B., & Pei, D. (2022) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2021.0605 · Cited by 21

The Arabidopsis Cop9 signalosome subunit 4 (CSN4) is involved in adventitious root formation

PACURAR, D. I., Păcurar, M. L., Lakehal, A., Păcurar, A. M., Ranjan, A., & Bellini, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-00744-1 · Cited by 21

Desmosomes: emerging pathways and non-canonical functions in cardiac arrhythmias and disease

Zhang, J., Liang, Y., Bradford, W. H., & Sheikh, F. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00829-2 · Cited by 21

Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN+ Proteases

Cao, S., Engilberge, S., Girard, É., Gabel, F., Franzetti, B., & Maupin-furlow, J. A. (2017) · Structure · doi:10.1016/j.str.2017.04.002 · Cited by 21

COP9 signalosome complex subunit 5, an IFT20 binding partner, is essential to maintain male germ cell survival and acrosome biogenesis†

Huang, Q., Liu, H., Zeng, J., Li, W., Zhang, S., Zhang, L., Song, S., Zhou, T., Sutovsky, M., Šutovský, P., et al. (2019) · Biology of Reproduction · doi:10.1093/biolre/ioz154 · Cited by 19

The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics

Llerena Schiffmacher, D. A., Lee, S.-H., Kliza, K. W., Theil, A. F., Akita, M., Helfricht, A., Bezstarosti, K., Gonzalo-Hansen, C., van Attikum, H., Verlaan-de Vries, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50584-7 · 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

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

Discovery of Monovalent Direct Degraders of BRD4 that Act via the Recruitment of DCAF11

Parker, G. S., Toth, J. I., Fish, S., Blanco, G., Kampert, T., Li, X., Yang, L., Stumpf, C. R., Steadman, K., Jamborcic, A., et al. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-24-0219 · Cited by 18

Timely upstream events regulating nucleotide excision repair by ubiquitin-proteasome system: ubiquitin guides the way

Chauhan, A. K., Sun, Y., Zhu, Q., & Wani, A. A. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103128 · Cited by 18

Electron cryomicroscopy as a powerful tool in biomedical research

Quentin, D., & Raunser, S. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-018-1640-y · Cited by 16

Integration of Fungus-Specific CandA-C1 into a Trimeric CandA Complex Allowed Splitting of the Gene for the Conserved Receptor Exchange Factor of CullinA E3 Ubiquitin Ligases in Aspergilli

Köhler, A. M., Harting, R., Langeneckert, A. E., Valerius, O., Gerke, J., Meister, C., Strohdiek, A., & Braus, G. H. (2019) · mBio · doi:10.1128/mbio.01094-19 · Cited by 15

The necessity of NEDD8/Rub1 for vitality and its association with mitochondria-derived oxidative stress

Pick, E. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101765 · Cited by 17

Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases

Bolhuis, D. L., Emanuele, M. J., & Brown, N. G. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230454 · Cited by 15

Cullin-RING Ligase 4 in Cancer: Structure, Functions, and Mechanisms

Cheng, J., Bin, X., & Tang, Z. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189169 · Cited by 18

Mechanisms of transcription-coupled repair and DNA damage surveillance in health and disease

van Sluis, M., Gonzalo-Hansen, C., Li, Q., Lans, H., Wang, D., & Marteijn, J. A. F. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00915-3 · Cited by 21

Neddylation Alleviates Methicillin-Resistant Staphylococcus aureus Infection by Inducing Macrophage Reactive Oxygen Species Production

Xiu, H., Peng, Y., Huang, X., Gong, J., Yang, J., Cai, J., Zhang, K., Cui, W., Shen, Y., Wang, J., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001167 · Cited by 14

The molecular determinants for distinguishing between ubiquitin and NEDD8 by USP2

Shin, Y., Chen, J.-H., & Chang, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-02322-x · Cited by 15

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

CSN1 facilitates proliferation and migration of hepatocellular carcinoma cells by upregulating cyclin A2 expression

Fu, H., Zhang, Y., Chen, Y., Chen, J., & Chen, P. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11684 · Cited by 14

Overexpression of COP9 signalosome subunits, CSN7A and CSN7B, exerts different effects on adipogenic differentiation

Huang, X., Ordemann, J., Pratschke, J., & Dubiel, W. (2016) · FEBS Open Bio · doi:10.1002/2211-5463.12129 · Cited by 14

Trade-off and flexibility in the dynamic regulation of the cullin-RING ubiquitin ligase repertoire

Straube, R., Shah, M., Flockerzi, D., & Wolf, D. A. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005869 · Cited by 14

Are Inositol Polyphosphates the Missing Link in Dynamic Cullin RING Ligase Regulation by the COP9 Signalosome?

Zhang, X., & Rao, F. (2019) · Biomolecules · doi:10.3390/biom9080349 · Cited by 13

Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

Qiao, S., Lee, C., Sherpa, D., Chrustowicz, J., Cheng, J., Duennebacke, M., Steigenberger, B. A., Karayel, Ö., Vu, D. T., von Gronau, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30803-9 · Cited by 13

IKK-Mediated Regulation of the COP9 Signalosome via Phosphorylation of CSN5

Zhang, J., Zhao, R., Yu, C., Bryant, C. L. N., Wu, K. K.-Y., Liu, Z., Ding, Y., Zhao, Y., Xue, B., Pan, Z., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00626 · Cited by 13

Oxygen-dependent regulation of E3(SCF)ubiquitin ligases and a Skp1-associated JmjD6 homolog in development of the social amoeba Dictyostelium

Boland, A. W., Gas‐Pascual, E., Nottingham, B. L., van der Wel, H., Daniel, N. G., Sheikh, M. O., Schafer, C. M., & West, C. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102305 · Cited by 11

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

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

The Proteasome Lid Triggers COP9 Signalosome Activity during the Transition of Saccharomyces cerevisiae Cells into Quiescence

Bramasole, L., Sinha, A., Harshuk-Shabso, D., Cirigliano, A., Gurevich, S. Z., Yu, Z., Carmeli, R., Glickman, M. H., Rinaldi, T., & Pick, E. (2019) · Biomolecules · doi:10.3390/biom9090449 · Cited by 10

Knockdown of COPS3 inhibits the progress of prostate cancer through reducing phosphorylated p38 MAPK expression and impairs the epithelial‐mesenchymal transition process

Zhu, Z., Hong, Y., Zhang, F., An, L., Yang, Q., Huang, X., & Xu, Q. (2019) · The Prostate · doi:10.1002/pros.23907 · Cited by 10

COP9 signalosome subunits protect Capicua from MAPK-dependent and -independent mechanisms of degradation

Suisse, A., He, D., Legent, K., & Treisman, J. E. (2017) · Development · doi:10.1242/dev.148767 · Cited by 10

Deneddylating enzyme SENP8 regulates neuronal development

Song, J., Kang, M., Lee, S., Kim, J., Park, S.-H., Park, D., Lee, S., & Suh, Y. H. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15797 · Cited by 9

Latent CSN-CRL complexes are crucial for curcumin-induced apoptosis and recruited during adipogenesis to lipid droplets via small GTPase RAB18

Dubiel, D., Wang, J., Hartig, R., Chaithongyot, S., Dubiel, W., & Naumann, M. (2023) · iScience · doi:10.1016/j.isci.2023.106468 · Cited by 9

CSN7B defines a variant COP9 signalosome complex with distinct function in DNA damage response

Wang, J., Dubiel, D., Wu, Y., Cheng, Y., Wolf, D. A., & Dubiel, W. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108662 · Cited by 9

Chromatin structure related to oncogenesis

Matsumoto, S., Horikoshi, N., Takizawa, Y., & Kurumizaka, H. (2023) · Cancer Science · doi:10.1111/cas.15850 · Cited by 8

Transcription‐coupled repair: tangled up in convoluted repair

Schiffmacher, D. A. L., Pai, Y. J., Pines, A., & Vermeulen, W. (2025) · FEBS Journal · doi:10.1111/febs.70104 · Cited by 10

CSN5i-3 is an orthosteric molecular glue inhibitor of COP9 signalosome

Shi, H., Wang, X., Yu, C., Mao, H., Jiao, F., Braitbard, M., Shor, B., Zhang, Z., Hinds, T. R., Cao, S., et al. (2026) · Nature · doi:10.1038/s41586-026-10129-y · Cited by 8

NUMB facilitates autophagy initiation through targeting SCFβ-TrCP2 complex

Li, H., Shu, S., Zhou, M., Chen, Y., Xiao, A., Ma, Y., Zhu, F., Hu, Z., & Nie, J. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00930-3 · Cited by 8

Regulatory Mechanism of the Constitutive Photomorphogenesis 9 Signalosome Complex in Response to Abiotic Stress in Plants

Wang, D., Musazade, E., Wang, H., Liu, J., Zhang, C., Liu, W., Liu, Y., & Guo, L. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c07224 · Cited by 8

Hormone profiling and the root proteome analysis of itpk1 mutant seedlings of barley (Hordeum vulgare) during the red-light induced photomorphogenesis

Vlčko, T., Tarkowská, D., Široká, J., Pěnčík, A., Simerský, R., Chamrád, I., Lenobel, R., Novák, O., & Ohnoutková, L. (2023) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2023.105428 · Cited by 8

COP9 Signalosome Subunit 3 Restricts Neuroinflammatory Responses During Cerebral Ischemia/Reperfusion Injury Through Stabilizing Suppressor of Cytokine Signaling 3 Protein

Liang, E. Y., Li, X., Fu, W., Zhao, C., Yang, B., & Yang, Z. (2021) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s298966 · Cited by 8

Analysis of expression profiles and prognostic value of COP9 signalosome subunits for patients with head and neck squamous cell carcinoma

Zhou, H., Sun, W., & Zou, J. (2021) · Oncology Letters · doi:10.3892/ol.2021.13064 · Cited by 8

Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex

Martínez, C., Iniesto, E., García-León, M., García-Corredera, D., Fonseca, S., Santiago, C., Yang, M., Yu, R., Chen, H., Altmann, E., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114802 · Cited by 7

The ubiquitin-proteasome system and chromosome 17 in cerebellar granule cells and medulloblastoma subgroups

Vriend, J. P., & Marzban, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2354-3 · Cited by 9

Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

Horváth, A., Róna, G., Pagano, M., & Jordan, P. W. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00278-x · Cited by 8

The COP9 signalosome inhibits Cullin-RING E3 ubiquitin ligases independently of its deneddylase activity

Suisse, A., Békés, M., Huang, T. T., & Treisman, J. E. (2018) · Fly · doi:10.1080/19336934.2018.1429858 · Cited by 7

HSC70 coordinates COP9 signalosome and SCF ubiquitin ligase activity to enable a prompt stress response

Nishimura, S., Kioka, H., Ding, S., Hakui, H., Shinomiya, H., Tanabe, K., Hitsumoto, T., Matsuoka, K., Kato, H., Tsukamoto, O., et al. (2025) · EMBO Reports · doi:10.1038/s44319-025-00376-x · Cited by 6

Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation

Park, Y.-H., Jeong, S., Ha, K., Yu, H. S., & Jang, S. B. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.5.201 · Cited by 6

Regulation of Cullin-RING E3 ligase dynamics by Inositol hexakisphosphate

Scott, D. C., & Kleiger, G. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001683117 · Cited by 6

Structural basis of Cullin-2 RING E3 ligase regulation by the COP9 signalosomePreprint

Faull, S. V., Lau, A. M. C., Martens, C., Ahdash, Z., Yébenes, H., Schmidt, C., Beuron, F., Cronin, N., Morris, E. P., & Politis, A. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/483024 · Cited by 6

DET1 dynamics underlie cooperative ubiquitination by CRL4 DET1-COP1 complexes

Burgess, A. E., Loughran, T. A., Turk, L. S., Nyvall, H. G., Dunlop, J. L., Jamieson, S. A., Curry, J. R., Burke, J. E., Filipčík, P., Brown, S. H. J., et al. (2025) · Science Advances · doi:10.1126/sciadv.adq4187 · Cited by 5

SOCS2 Binds to and Regulates EphA2 through Multiple Mechanisms

Pilling, C., & Cooper, J. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-11040-3 · Cited by 5

Cereblon-Targeting Ligase Degraders in Myeloma

Lee, H., Neri, P. E., & Bahlis, N. J. (2024) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2024.01.001 · Cited by 5

Multi-omics analysis reveals RNA polymerase II degradation as a novel mechanism of PF-3758309’s anti-tumor activity

Jia, X., Zhang, J., Pan, L., He, J., Zhu, M., Zhao, L., Zhang, X., Zhao, W., Xie, D., Shen, X., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02677-5 · Cited by 4

ROS disrupt COP9 signalosome-mediated ABCA1 protection and trigger its ubiquitination and degradation by cullin3 inhibiting cholesterol efflux and promoting foam cell formation in response to GPCR agonists

Govatati, S., Yadavalli, C. S., Traylor, J. G., Orr, A. W., & Rao, G. N. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104095 · Cited by 4

The Emerging Role of CSN6 in Biological Behavior and Cancer Progress

Mao, Z., Cheng, C., & Pei, D. (2019) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520619666190408142131 · Cited by 4

COP9 signalosome complex is a prognostic biomarker and corresponds with immune infiltration in hepatocellular carcinoma

Liu, J., Han, D., Xuan, J., Xie, J., Wang, W., Zhou, Q., & Chen, K. (2024) · Aging · doi:10.18632/aging.205646 · Cited by 4

Investigating the binding mechanism of piperidinyl ureas inhibitors based on the UBC12-DCN1 interaction by 3D-QSAR, molecular docking and molecular dynamics simulations

Zhao, J., Zang, J., Yang, J. C., Gao, Q.-B., Yan, Y., Ma, C.-Y., Chen, Y., Ding, L., & Liu, H. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1841678 · Cited by 4

The COP9 Signalosome Variant CSNCSN7A Stabilizes the Deubiquitylating Enzyme CYLD Impeding Hepatic Steatosis

Huang, X., Dubiel, D., & Dubiel, W. (2021) · Livers · doi:10.3390/livers1030011 · Cited by 4

Antibody-free approach for ubiquitination profiling by selectively clicking the ubiquitination sites

Sun, M., Zhang, Q., Zhao, B., Huang, Q., Wu, W., Fan, P., Zhang, X., & Zhang, X. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.340877 · Cited by 4

The COP9 signalosome variants CSNCSN7A and CSNCSN7B form complexes with specific CRLs which are targets of autophagy

Dubiel, W., & Dubiel, D. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253018 · Cited by 3

Extracellular granzyme K enhances PD-L1 transcription and stability via F2RL1 activation to facilitate tumor immune evasion in lung adenocarcinoma

Feng, H., Ye, Z., Zhai, K., Li, B., Song, T.-N., Meng, Y.-Q., Huang, H., Li, Z., Cui, B.-Q., Yang, N., et al. (2026) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2025-013170 · Cited by 3

Native mass spectrometry for proximity-inducing compounds: a new opportunity for studying chemical-induced protein modulation

Fabbrizi, E., Fiorentino, F., Casano, F., Mai, A., & Rotili, D. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2486146 · Cited by 3

Inactivation of Cops5 in Smooth Muscle Cells Causes Abnormal Reproductive Hormone Homeostasis and Development in Mice

Huang, Q., Man, Y., Li, W., Zhou, Q., Yuan, S., Yap, Y. T., Nayak, N., Zhang, L., Song, S., Dunbar, J. C., et al. (2023) · Endocrinology · doi:10.1210/endocr/bqad062 · Cited by 3

Can we develop effective direct or indirect inhibitors of transcription factors? On the clinical evolution of protein degraders for multiple myeloma therapy

Meli, R., Aksoy, O., Vallet, S., Slade, D., & Podar, K. (2025) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2025.2482557 · Cited by 2

The role of neddylation in colorectal cancer and its therapeutic potential

Mi, C., Cui, F., Wang, S., Du, Y., Li, Y., & Yang, H. (2025) · Discover Oncology · doi:10.1007/s12672-025-04264-7 · Cited by 2

Structural basis of CSN-mediated SCF deneddylation

Ding, S., Clapperton, J. A., Mäeots, M.-E., Kunzelmann, S., Shaaban, M., & Enchev, R. I. (2026) · Nature Communications · doi:10.1038/s41467-025-67566-y · Cited by 2

A Novel CSN5 Inhibitor Drives Tumor-Intrinsic PD-L1 Degradation and Exerts Direct Antitumor Efficacy in Triple-Negative Breast Cancer

Wang, Y., Lei, H., Liu, W., Li, X., Jiang, S., Zhang, H., Xiong, R., Yang, Z., Yan, Y., Jiang, Y., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02669 · Cited by 2

Single-Particle Electron Microscopy Analysis of DNA Repair Complexes

Sawicka, M., Aramayo, R. J., Ayala, R., Glyde, R., & Zhang, X. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.03.010 · Cited by 2

Saccharomyces cerevisiae as a Toolkit for COP9 Signalosome Research

Harshuk-Shabso, D., Castel, N., Israeli, R., Harari, S., & Pick, E. (2021) · Biomolecules · doi:10.3390/biom11040497 · Cited by 1

Suppressors of Break-Induced Replication in Human Cells

Rider, S. D., Damewood, F. J., Gadgil, R. Y., Hitch, D. C., Alhawach, V., Shrestha, R., Shanahan, M., Zavada, N., & Leffak, M. (2023) · Genes · doi:10.3390/genes14020398 · Cited by 2

Preparation of Proteins and Macromolecular Assemblies for Cryo-electron Microscopy

Brillault, L., & Landsberg, M. J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9869-2_13 · Cited by 2

Activity-based profiling of cullin-RING ligase networks by conformation-specific probesPreprint

Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., & Schulman, B. A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.14.524048 · Cited by 2

KDM5B cooperates with CRL4B complex to promote the tumorigenesis of ER+ breast cancer via regulating cholesterol metabolism

Yang, Y., Gao, T., Yuan, B., Hao, X., Huo, M., Hu, T., Ma, T., Zhang, M., Zhang, D., Teng, X., et al. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08438-1 · Cited by 1

Molecular mechanisms of DNA damage recognition and chromatin dynamics regulating mammalian nucleotide excision repair

Kusakabe, M., & Sugasawa, K. (2026) · DNA repair · doi:10.1016/j.dnarep.2026.103951 · Cited by 1

Comparison of two UPS regulators: the 26S proteasome LID and the COP9 signalosome

Dubiel, D., & Dubiel, W. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1496862 · Cited by 1

Molecular Mechanism of DNA Damage Recognition for Global Genomic Nucleotide Excision Repair: A Defense System Against UV-Induced Skin Cancer

Sugasawa, K. (2018) · Springer eBooks · doi:10.1007/978-981-10-6722-8_1 · Cited by 1

Azaindoles as Zinc‐Binding Small‐Molecule Inhibitors of the JAMM Protease CSN5

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Finding Pathogenic nsSNP’s and their structural effect on COPS2 using Molecular Dynamic ApproachPreprint

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Voting Rights and Freedom of Speech Decisions from the October 2007 Term

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Faculty Opinions recommendation of Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15.

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Faculty Opinions recommendation of DNA damage detection in nucleosomes involves DNA register shifting.

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Faculty Opinions recommendation of DNA damage detection in nucleosomes involves DNA register shifting.

Lebbink, J. H. G. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.735843093.793562917

Faculty Opinions recommendation of DNA damage detection in nucleosomes involves DNA register shifting.

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Novel functions of LUBAC-mediated M1 poly-ubiquitination in TNFR1-mediated necroptosis

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Targeting the COP9 signalosome overcomes platinum resistance in ovarian cancer through two distinct genome stability mechanismsPreprint

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Additional file 1 of Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

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Additional file 3 of Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

Horváth, A., Róna, G., Pagano, M., & Jordan, P. W. (2020) · Figshare · doi:10.6084/m9.figshare.12276836

Additional file 2 of Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

Horváth, A., Róna, G., Pagano, M., & Jordan, P. W. (2020) · Figshare · doi:10.6084/m9.figshare.12276827

Additional file 5 of Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

Horváth, A., Róna, G., Pagano, M., & Jordan, P. W. (2020) · Figshare · doi:10.6084/m9.figshare.12276842

Additional file 4 of Interaction between NSMCE4A and GPS1 links the SMC5/6 complex to the COP9 signalosome

Horváth, A., Róna, G., Pagano, M., & Jordan, P. W. (2020) · Figshare · doi:10.6084/m9.figshare.12276839

Crystal structure of the human COP9 signalosome

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Structural basis of Cullin-2 RING E3 ligase regulation by the COP9 signalosomePreprint

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Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activity

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The COP9 signalosome: A versatile regulatory hub of Cullin-RING ligases

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