COP9 Signalosome

Auxin regulates SCFTIR1-dependent degradation of AUX/IAA proteins

Gray, W. M., Kepinski, S., Rouse, D. T., Leyser, O., & Estelle, M. A. (2001) · Nature · doi:10.1038/35104500 · Cited by 1,415

Targeted destabilization of HY5 during light-regulated development of Arabidopsis

Østerlund, M. T., Hardtke, C. S., Wei, N., & Deng, X. W. (2000) · Nature · doi:10.1038/35013076 · Cited by 1,363

SCF and Cullin/RING H2-Based Ubiquitin Ligases

Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238

The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage

Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J.-I., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., & Nakatani, Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00316-7 · Cited by 756

Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

Lyapina, S., Cope, G. A., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D. A., Wei, N., Shevchenko, A., & Deshaies, R. J. (2001) · Science · doi:10.1126/science.1059780 · Cited by 699

Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1

Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075901 · Cited by 682

Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1

Tomoda, K., Kubota, Y., & Kato, J. (1999) · Nature · doi:10.1038/18230 · Cited by 632

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612

The RAR1 Interactor SGT1, an Essential Component of R Gene-Triggered Disease Resistance

Azevedo, C., Sadanandom, A., Kitagawa, K., Freialdenhoven, A., Shirasu, K., & Schulze‐Lefert, P. (2002) · Science · doi:10.1126/science.1067554 · Cited by 611

Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1

Kleemann, R., Haußer, A., Geiger, G., Mischke, R., Burger‐Kentischer, A., Flieger, O., Johannes, F., Roger, T., Calandra, T., Kapurniotu, A., et al. (2000) · Nature · doi:10.1038/35041591 · Cited by 567

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

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523

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

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

A Genome-wide RNAi Screen Identifies Multiple Synthetic Lethal Interactions with the Ras Oncogene

Luo, J., Emanuele, M. J., Li, D., Creighton, C. J., Schlabach, M. R., Westbrook, T. F., Wong, K.-K., & Elledge, S. J. (2009) · Cell · doi:10.1016/j.cell.2009.05.006 · Cited by 1,017

Ubiquitin and ubiquitin-like proteins as multifunctional signals

Welchman, R., Gordon, C., & Mayer, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1700 · Cited by 849

Stabilization of Snail by NF-κB Is Required for Inflammation-Induced Cell Migration and Invasion

Wu, Y., Deng, J., Rychahou, P. G., Qiu, S., Evers, B. M., & Zhou, B. P. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.016 · Cited by 814

Dual roles of Nrf2 in cancer

LAU, A., VILLENEUVE, N., Sun, Z., Wong, P. K., & Zhang, D. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.09.003 · Cited by 653

Drug discovery in the ubiquitin–proteasome system

Nalepa, G., Rolfe, M., & Harper, J. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2056 · Cited by 635

The Ubiquitin-Proteasome Pathway and Plant Development

Moon, J., Parry, G., & Estelle, M. A. (2004) · The Plant Cell · doi:10.1105/tpc.104.161220 · Cited by 597

SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

Banerjee, A. K., Blanco, M. R., Bruce, E. A., Honson, D. D., Chen, L. M., Chow, A., Bhat, P., Ollikainen, N., Quinodoz, S. A., Loney, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.004 · Cited by 583

Coordination of secondarymetabolism and development in fungi: the velvet familyof regulatory proteins

Bayram, Ö., & Braus, G. H. (2011) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2011.00285.x · Cited by 551

Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways

Zhao, C., Denison, C., Huibregtse, J. M., Gygi, S. P., & Krug, R. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504754102 · Cited by 478

Nedd8 on cullin: building an expressway to protein destruction

Pan, Z., Kentsis, A., Dias, D. C., Yamoah, K., & Wu, K. (2004) · Oncogene · doi:10.1038/sj.onc.1207414 · Cited by 436

Deubiquitylases From Genes to Organism

Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 439

Regulation of the Nrf2–Keap1 Antioxidant Response by the Ubiquitin Proteasome System: An Insight into Cullin-Ring Ubiquitin Ligases

Villeneuve, N. F., Lau, A., & Zhang, D. D. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3211 · Cited by 423

Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics

Bennett, E. J., Rush, A. J., Gygi, S. P., & Harper, J. W. (2010) · Cell · doi:10.1016/j.cell.2010.11.017 · Cited by 388

ArabidopsisCONSTANS-LIKE3 Is a Positive Regulator of Red Light Signaling and Root Growth

Datta, S., Hettiarachchi, C. M., Deng, X., & Holm, M. (2005) · The Plant Cell · doi:10.1105/tpc.105.038182 · Cited by 371

AMSH is an endosome-associated ubiquitin isopeptidase

McCullough, J., Clague, M. J., & Urbé, S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401141 · Cited by 369

Human De-Etiolated-1 Regulates c-Jun by Assembling a CUL4A Ubiquitin Ligase

Wertz, I. E., O’Rourke, K. M., Zhang, Z., Dornan, D., Arnott, D. P., Deshaies, R. J., & Dixit, V. M. (2004) · Science · doi:10.1126/science.1093549 · Cited by 365

Function and regulation of protein neddylation

Rabut, G. E. E., & Peter, M. (2008) · EMBO Reports · doi:10.1038/embor.2008.183 · Cited by 360

Building and remodelling Cullin–RING E3 ubiquitin ligases

Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327

The DDB1-CUL4A DDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites

Kapetanaki, M. G., Guerrero‐Santoro, J., Bisi, D. C., Hsieh, C. L., Rapić-Otrin, V., & Levine, A. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511160103 · Cited by 323

APC/C and SCF: Controlling Each Other and the Cell Cycle

Vodermaier, H. C. (2004) · Current Biology · doi:10.1016/j.cub.2004.09.020 · Cited by 323

Specific Patterns of Electrophile Adduction Trigger Keap1 Ubiquitination and Nrf2 Activation

Hong, F., Sekhar, K. R., Freeman, M. L., & Liebler, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503346200 · Cited by 316

Cullin-RING ubiquitin ligases: global regulation and activation cycles

Bosu, D. R., & Kipreos, E. T. (2008) · Cell Division · doi:10.1186/1747-1028-3-7 · Cited by 318

Ubiquitination of Keap1, a BTB-Kelch Substrate Adaptor Protein for Cul3, Targets Keap1 for Degradation by a Proteasome-independent Pathway

Zhang, D. D., Lo, S., Sun, Z., Habib, G. M., Lieberman, M. W., & Hannink, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501279200 · Cited by 299

Dynamic Integration of Auxin Transport and Signalling

Leyser, O. (2006) · Current Biology · doi:10.1016/j.cub.2006.05.014 · Cited by 280

Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases

Goldenberg, S. J., Cascio, T. C., Shumway, S. D., Garbutt, K. C., Liu, J., Xiong, Y., & Zheng, N. (2004) · Cell · doi:10.1016/j.cell.2004.10.019 · Cited by 280

Regulation of DNA repair by ubiquitylation

Huang, T. T., & D’Andrea, A. D. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1908 · Cited by 279

Commensal bacteria modulate cullin‐dependent signaling via generation of reactive oxygen species

Kumar, A., Wu, H., Collier-Hyams, L. S., Hansen, J. M., Li, T., Yamoah, K., Pan, Z., Jones, D. P., & Neish, A. S. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601867 · Cited by 268

Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins

Pierce, N. W., Lee, J. E., Liu, X., Sweredoski, M. J., Graham, R. L. J., Larimore, E. A., Rome, M., Zheng, N., Clurman, B. E., Hess, S., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.024 · Cited by 262

Identification of pathways regulating cell size and cell-cycle progression by RNAi

Björklund, M., Taipale, M., Varjosalo, M. T., Saharinen, J., Lahdenperä, J., & Taipale, J. (2006) · Nature · doi:10.1038/nature04469 · Cited by 257

Review of Molecular Mechanisms Involved in the Activation of the Nrf2-ARE Signaling Pathway by Chemopreventive Agents

Giudice, A., Arra, C., & Turco, M. C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_3 · Cited by 254

Targeting Neddylation Pathways to Inactivate Cullin-RING Ligases for Anticancer Therapy

Zhao, Y., Morgan, M. A., & Sun, Y. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5795 · Cited by 244

Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation

Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237

Genetic regulators of large-scale transcriptional signatures in cancer

Adler, A. S., Lin, M., Horlings, H. M., Nuyten, D. S. A., van de Vijver, M. J., & Chang, H. Y. (2006) · Nature Genetics · doi:10.1038/ng1752 · Cited by 232

E3 Ubiquitin Ligases as Regulators of Membrane Protein Trafficking and Degradation

d’Azzo, A., Bongiovanni, A., & Nastasi, T. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00294.x · Cited by 228

Plant E3 Ligases: Flexible Enzymes in a Sessile World

Chen, L., & Hellmann, H. A. (2013) · Molecular Plant · doi:10.1093/mp/sst005 · Cited by 220

Regulation of Cullin RING Ligases

Hotton, S. K., & Callis, J. (2007) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.58.032806.104011 · Cited by 214

Structural Organization of the 19S Proteasome Lid: Insights from MS of Intact Complexes

Sharon, M., Taverner, T., Ambroggio, X. I., Deshaies, R. J., & Robinson, C. V. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040267 · Cited by 210

SUMO modification of the ubiquitin-conjugating enzyme E2-25K

Pichler, A., Knipscheer, P., Oberhofer, E., van Dijk, W. J., Körner, R., Olsen, J. V., Jentsch, S., Melchior, F., & Sixma, T. K. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb903 · Cited by 208

MIF-Dependent Control of Tumor Immunity

Noe, J. T., & Mitchell, R. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.609948 · Cited by 198

CSN controls NF‐κB by deubiquitinylation of IκBα

Schweitzer, K., Bozko, P. M., Dubiel, W., & Naumann, M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601600 · Cited by 197

Targeted inhibition of the COP9 signalosome for treatment of cancer

Schlierf, A., Altmann, E., Quancard, J., Jefferson, A. B., Assenberg, R., Renatus, M., Jones, M. D., Hassiepen, U., Schaefer, M., Kiffe, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms13166 · Cited by 188

Isolation of Mammalian 26S Proteasomes and p97/VCP Complexes Using the Ubiquitin-like Domain from HHR23B Reveals Novel Proteasome-Associated Proteins

Besche, H. C., Haas, W., Gygi, S. P., & Goldberg, A. L. (2009) · Biochemistry · doi:10.1021/bi802198q · Cited by 187

Protein partners of deubiquitinating enzymes

Ventii, K., & Wilkinson, K. D. (2008) · Biochemical Journal · doi:10.1042/bj20080798 · Cited by 186

CSN facilitates Cullin–RING ubiquitin ligase function by counteracting autocatalytic adapter instability

Wee, S., Geyer, R. K., Toda, T., & Wolf, D. A. (2005) · Nature Cell Biology · doi:10.1038/ncb1241 · Cited by 183

Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation

Wu, J., Lin, H., Hu, Y.-C., & Chien, C. (2005) · Nature Cell Biology · doi:10.1038/ncb1301 · Cited by 183

Curcumin induces stabilization of Nrf2 protein through Keap1 cysteine modification

Shin, J. W., Chun, K., Kim, D., Kim, S., Kim, S. H., Cho, N.-C., Na, H., & Surh, Y. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113820 · Cited by 178

The COP9 signalosome regulates the Neurospora circadian clock by controlling the stability of the SCF FWD-1 complexPreprint

He, Q., Cheng, P., He, Q., & Liu, Y. (2005) · Genes & Development · doi:10.1101/gad.1322205 · Cited by 174

RNAi Screening Implicates a SKN-1–Dependent Transcriptional Response in Stress Resistance and Longevity Deriving from Translation Inhibition

Wang, J., Robida-Stubbs, S., Tullet, J. M. A., Rual, J.-F. M., Vidal, M., & Blackwell, T. K. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001048 · Cited by 169

Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels

Cope, G. A., & Deshaies, R. J. (2006) · BMC Biochemistry · doi:10.1186/1471-2091-7-1 · Cited by 176

How versatile are inositol phosphate kinases?

Shears, S. B. (2004) · Biochemical Journal · doi:10.1042/bj20031428 · Cited by 174

NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control

Wang, B., Hurov, K., Hofmann, K., & Elledge, S. J. (2009) · Genes & Development · doi:10.1101/gad.1770309 · Cited by 172

Regulating insulin signaling and β-cell function through IRS proteinsThis paper is one of a selection of papers published in this Special Issue, entitled Second Messengers and Phosphoproteins—12th International Conference.

White, M. F. (2006) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y06-008 · Cited by 164

Structural Basis for a Reciprocal Regulation between SCF and CSN

Enchev, R. I., Scott, D. C., da Fonseca, P. C. A., Schreiber, A., Monda, J. K., Schulman, B. A., Peter, M., & Morris, E. P. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.019 · Cited by 158

Symmetrical Modularity of the COP9 Signalosome Complex Suggests its Multifunctionality

Sharon, M., Mao, H., Erba, E. B., Stephens, E., Zheng, N., & Robinson, C. V. (2009) · Structure · doi:10.1016/j.str.2008.10.012 · Cited by 155

JAB1/CSN5: a new player in cell cycle control and cancer

Shackleford, T. J., & Claret, F. X. (2010) · Cell Division · doi:10.1186/1747-1028-5-26 · Cited by 155

Multiple Functions of Jab1 Are Required for Early Embryonic Development and Growth Potential in Mice

Tomoda, K., Yoneda‐Kato, N., Fukumoto, A., Yamanaka, S., & Kato, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406559200 · Cited by 155

The Zinc Finger of the CSN-Associated Deubiquitinating Enzyme USP15 Is Essential to Rescue the E3 Ligase Rbx1

Hetfeld, B. K. J., Helfrich, A., Kapelari, B., Scheel, H., Hofmann, K., Guterman, A., Glickman, M. H., Schade, R., Kloetzel, P., & Dubiel, W. (2005) · Current Biology · doi:10.1016/j.cub.2005.05.059 · Cited by 149

Development, structure, and maintenance of C. elegans body wall muscle

Gieseler, K. (2016) · WormBook · doi:10.1895/wormbook.1.81.2 · Cited by 142

Role of the MPN Subunits in COP9 Signalosome Assembly and Activity, and Their Regulatory Interaction with Arabidopsis Cullin3-Based E3 Ligases

Gusmaroli, G., Figueroa, P. M., Serino, G., & Deng, X. W. (2007) · The Plant Cell · doi:10.1105/tpc.106.047571 · Cited by 147

PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes

Zhou, C., Arslan, F., Wee, S., Krishnan, S., Ivanov, A. R., Oliva, A., Leatherwood, J., & Wolf, D. A. (2005) · BMC Biology · doi:10.1186/1741-7007-3-14 · Cited by 147

Mammalian COP9 signalosome

Kato, J., & Yoneda‐Kato, N. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01349.x · Cited by 145

Roles of COP9 signalosome in cancer

Lee, M., Zhao, R., Phan, L. M., & Yeung, S. J. (2011) · Cell Cycle · doi:10.4161/cc.10.18.17320 · Cited by 137

Role of MIF in Inflammation and Tumorigenesis

Bach, J., Rinn, B., Meyer, B., Dodel, R. C., & Bacher, M. (2008) · Oncology · doi:10.1159/000155223 · Cited by 138

Arabidopsis CAND1, an Unmodified CUL1-Interacting Protein, Is Involved in Multiple Developmental Pathways Controlled by Ubiquitin/Proteasome-Mediated Protein Degradation

Feng, S., Shen, Y., Sullivan, J. A., Rubio, V., Xiong, Y., Sun, T., & Deng, X. W. (2004) · The Plant Cell · doi:10.1105/tpc.021949 · Cited by 141

The Bacterial Fermentation Product Butyrate Influences Epithelial Signaling via Reactive Oxygen Species-Mediated Changes in Cullin-1 Neddylation

Kumar, A., Wu, H., Collier-Hyams, L. S., Kwon, Y.-M., Hanson, J. M., & Neish, A. S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.1.538 · Cited by 135

The utility F-box for protein destruction

Ho, M. S.-C., Ou, C.-Y., Chan, Y., Chien, C., & Pi, H. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7592-6 · Cited by 132

Regulation of neddylation and deneddylation of cullin1 in SCF Skp2 ubiquitin ligase by F-box protein and substrate

Bornstein, G., Ganoth, D., & Hershko, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603921103 · Cited by 128

Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy.

Higa, L. A., & Zhang, H. (2007) · Cell Division · doi:10.1186/1747-1028-2-5 · Cited by 126

Endothelin Receptor Signaling: New Insight Into Its Regulatory Mechanisms

Horinouchi, T., Terada, K., Higashi, T., & Miwa, S. (2013) · Journal of Pharmacological Sciences · doi:10.1254/jphs.13r02cr · Cited by 122

F-Box-Directed CRL Complex Assembly and Regulation by the CSN and CAND1

Schmidt, M. W., McQuary, P. R., Wee, S., Hofmann, K., & Wolf, D. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.024 · Cited by 125

Adenosine and Hypoxia-Inducible Factor Signaling in Intestinal Injury and Recovery

Colgan, S. P., & Eltzschig, H. K. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020911-153230 · Cited by 123

USP15 Negatively Regulates Nrf2 through Deubiquitination of Keap1

Villeneuve, N. F., Tian, W., Wu, T., Sun, Z., Lau, A., Chapman, E., Fang, D., & Zhang, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.022 · Cited by 120

Plasticity of the Cullin-RING Ligase Repertoire Shapes Sensitivity to Ligand-Induced Protein Degradation

Mayor-Ruiz, C., Jaeger, M. G., Bauer, S., Brand, M., Sin, C., Hanzl, A., Mueller, A. C., Menche, J., & Winter, G. E. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.013 · Cited by 119

COP9 signalosome: Discovery, conservation, activity, and function

Qin, N., Xu, D., Li, J., & Deng, X. W. (2020) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12903 · Cited by 119

Cutting Edge: Bacterial Modulation of Epithelial Signaling via Changes in Neddylation of Cullin-1

Collier-Hyams, L. S., Sloane, V. M., Batten, B. C., & Neish, A. S. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.7.4194 · Cited by 119

Lessons from Fungal F-Box Proteins

Jonkers, W., & Rep, M. (2009) · Eukaryotic Cell · doi:10.1128/ec.00386-08 · Cited by 110

Arabidopsis ETA2 , an Apparent Ortholog of the Human Cullin-Interacting Protein CAND1, Is Required for Auxin Responses Mediated by the SCF TIR1 Ubiquitin Ligase

Chuang, H.-W., Zhang, W., & Gray, W. M. (2004) · The Plant Cell · doi:10.1105/tpc.021923 · Cited by 112

A Genome-wide Screen Identifies p97 as an Essential Regulator of DNA Damage-Dependent CDT1 Destruction

Raman, M., Havens, C. G., Walter, J. C., & Harper, J. W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.036 · Cited by 112

The Arabidopsis CSN5A and CSN5B Subunits Are Present in Distinct COP9 Signalosome Complexes, and Mutations in Their JAMM Domains Exhibit Differential Dominant Negative Effects on Development

Gusmaroli, G., Feng, S., & Deng, X. W. (2004) · The Plant Cell · doi:10.1105/tpc.104.025999 · Cited by 109

AtCAND1, A HEAT-Repeat Protein That Participates in Auxin Signaling in Arabidopsis

Cheng, Y., Dai, X., & Zhao, Y. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.044495 · Cited by 107

RAC GTPases in Tobacco and Arabidopsis Mediate Auxin-Induced Formation of Proteolytically Active Nuclear Protein Bodies That Contain AUX/IAA Proteins

Tao, L., Cheung, A. Y., Nibau, C., & Wu, H. (2005) · The Plant Cell · doi:10.1105/tpc.105.032987 · Cited by 109

Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers

Zhao, R., Yeung, S. J., Chen, J., Iwakuma, T., Su, C., Chen, B., Qu, C., Zhang, F., Chen, Y., Lin, Y., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44111 · Cited by 107

Revisiting the COP9 signalosome as a transcriptional regulator

Chamovitz, D. (2009) · EMBO Reports · doi:10.1038/embor.2009.33 · Cited by 106

CSN- and CAND1-dependent remodelling of the budding yeast SCF complex

Zemla, A., Thomas, Y., Kędziora, S., Knebel, A., Wood, N. T., Rabut, G. E. E., & Kurz, T. (2013) · Nature Communications · doi:10.1038/ncomms2628 · Cited by 102

CAND1-Mediated Substrate Adaptor Recycling Is Required for Efficient Repression of Nrf2 by Keap1

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Ddb1 controls genome stability and meiosis in fission yeastPreprint

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The cell cycle as a therapeutic target for Alzheimer's disease

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Substrate-mediated Regulation of Cullin Neddylation

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Control of Cullin-Ring Ubiquitin Ligase Activity by Nedd8

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Roles for CSN5 in control of p53/MDM2 activities

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Regulation of cullin-based ubiquitin ligases by the Nedd8/RUB ubiquitin-like proteins

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CSN5/Jab1 Is Involved in Ligand-Dependent Degradation of Estrogen Receptor α by the Proteasome

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A genome-scale CRISPR-Cas9 screening in myeloma cells identifies regulators of immunomodulatory drug sensitivity

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The COP9 signalosome

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The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?

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The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis

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The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development

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The COP9 signalosome: more than a protease

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