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

CSN5/Jab1 controls multiple events in the mammalian cell cycle

Yoshida, A., Yoneda‐Kato, N., Panattoni, M., Pardi, R., & Kato, J. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.10.039 · Cited by 35

Dysfunction of amyloid precursor protein signaling in neurons leads to DNA synthesis and apoptosis

Neve, R. L., & McPhie, D. L. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.008 · Cited by 33

Stable Form of JAB1 Enhances Proliferation and Maintenance of Hematopoietic Progenitors

Mori, M., Yoneda‐Kato, N., Yoshida, A., & Kato, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804539200 · Cited by 33

CSN5/Jab1 facilitates non-small cell lung cancer cell growth through stabilizing survivin

Li, J., Li, Y., Wang, B., Ma, Y., & Chen, P. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.183 · Cited by 32

Substrate Phosphorylation and Feedback Regulation in JFK-promoted p53 Destabilization

Sun, L., Shi, L., Wang, F., Huangyang, P., Si, W., Yang, J., Yao, Z., & Shang, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.195115 · Cited by 32

Crosstalk between the NF‐κB activating IKK‐complex and the CSN signalosome

Orel, L., Neumeier, H., Hochrainer, K., Binder, B. R., & Schmid, J. A. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00866.x · Cited by 32

The Organization of a CSN5-containing Subcomplex of the COP9 Signalosome

Kotiguda, G. G., Weinberg, D., Dessau, M., Salvi, C., Serino, G., Chamovitz, D., & Hirsch, J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.387977 · Cited by 33

Exposing the subunit diversity within protein complexes: A mass spectrometry approach

Rozen, S., Tieri, A., Ridner, G., Stark, A.-K., Schmaler, T., Ben‐Nissan, G., Dubiel, W., & Sharon, M. (2013) · Methods · doi:10.1016/j.ymeth.2012.12.013 · Cited by 31

CRL4 antagonizes SCFFbxo7-mediated turnover of cereblon and BK channel to regulate learning and memory

Song, T., Liang, S., Liu, J., Zhang, T., Yin, Y., Geng, C., Gao, S., Feng, Y., Xu, H., Guo, D., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007165 · Cited by 31

COP9 signalosome is an essential and druggable parasite target that regulates protein degradation

Ghosh, S., Farr, L. A., Singh, A., Leaton, L. A., Padalia, J., Shirley, D.-A. T., Sullivan, D. J., & Moonah, S. N. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008952 · Cited by 28

LKB1: An emerging therapeutic target for cardiovascular diseases

Molaei, A., Molaei, E., Sadeghnia, H. R., Hayes, A. W., & Karimi, G. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120844 · Cited by 30

COP9 signalosome controls the Carma1–Bcl10–Malt1 complex upon T‐cell stimulation

Welteke, V., Eitelhuber, A. C., Düwel, M., Schweitzer, K., Naumann, M., & Krappmann, D. (2009) · EMBO Reports · doi:10.1038/embor.2009.64 · Cited by 31

TCTP and CSN4 control cell cycle progression and development by regulating CULLIN1 neddylation in plants and animals

Betsch, L., Boltz, V., Brioudes, F., Pontier, G., Girard, V., Savarin, J., Wipperman, B., Chambrier, P., Tissot, N., Benhamed, M., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1007899 · Cited by 30

Depletion of Jab1 inhibits proliferation of pancreatic cancer cell lines

Fukumoto, A., Tomoda, K., Yoneda‐Kato, N., Nakajima, Y., & Kato, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.09.042 · Cited by 30

Control of NF-κB activation by the COP9 signalosome

Schweitzer, K., & Naumann, M. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380156 · Cited by 29

Perturbation of neddylation-dependent NF-κB responses in the intestinal epithelium drives apoptosis and inhibits resolution of mucosal inflammation

Ehrentraut, S., Curtis, V. F., Wang, R. X., Saeedi, B. J., Ehrentraut, H., Onyiah, J. C., Kelly, C. J., Campbell, E. L., Glover, L. E., Kominsky, D. J., et al. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0273 · Cited by 28

Cullin 4-DCAF Proteins in Tumorigenesis

Zhou, Z., Song, X., Wavelet, C. M., & Wan, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_15 · Cited by 29

Jab1 promotes gastric cancer tumorigenesis via non-ubiquitin proteasomal degradation of p14ARF

Wang, L., Du, W., Xie, M., Liu, M.-R., Huo, F., Yang, J., & Pei, D. (2020) · Gastric Cancer · doi:10.1007/s10120-020-01087-z · Cited by 28

CBS9106-Induced CRM1 Degradation Is Mediated by Cullin Ring Ligase Activity and the Neddylation Pathway

Saito, N., Sakakibara, K., Sato, T., Friedman, J. M., Kufe, D. W., VonHoff, D. D., & Kawabe, T. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0064 · Cited by 28

Herpes virus deneddylases interrupt the cullin-RING ligase neddylation cycle by inhibiting the binding of CAND1

Gastaldello, S., Callegari, S., Coppotelli, G., Hildebrand, S., Song, M., & Masucci, M. G. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs012 · Cited by 29

COP9 Limits Dendritic Branching via Cullin3-Dependent Degradation of the Actin-Crosslinking BTB-Domain Protein Kelch

Djagaeva, I., & Doronkin, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007598 · Cited by 28

Changes in the Hippocampal Proteome Associated with Spatial Memory Impairment after Exposure to Low (20 cGy) Doses of 1 GeV/n 56Fe Radiation

Britten, R. A., Jewell, J. S., Davis, L. K., Miller, V. D., Hadley, M. M., Semmes, O. J., Lónárt, G., & Dutta, S. M. (2017) · Radiation Research · doi:10.1667/rr14067.1 · Cited by 27

Nucleotide excision repair in chromatin: The shape of things to come

Reed, S. H. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.04.009 · 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

Adaptive exchange sustains cullin–RING ubiquitin ligase networks and proper licensing of DNA replication

Zhang, Y., Jost, M., Pak, R. A., Lu, D., Li, J., Lomenick, B., Garbis, S. D., Li, C.-M., Weissman, J. S., Lipford, J. R., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205608119 · Cited by 24

The JNK-Like MAPK KGB-1 ofCaenorhabditis ElegansPromotes Reproduction, Lifespan, and Gene Expressions for Protein Biosynthesis and Germline Homeostasis but Interferes with Hyperosmotic Stress Tolerance

Gerke, P., Keshet, A., Mertenskötter, A., & Paul, R. J. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000366392 · Cited by 25

CSN6, a subunit of the COP9 signalosome, is involved in early response to iron deficiency in Oryza sativa

Tan, S., Liu, F., Pan, X., Zang, Y., Jin, F., Zu, W.-X., Qi, X., Xiao, W., & Yin, L. (2016) · Scientific Reports · doi:10.1038/srep25485 · Cited by 25

ThecsnD/csnESignalosome Genes Are Involved in theAspergillus nidulansDNA Damage Response

Lima, J. F., Malavazi, I., Kress, M. R. V. Z., Savoldi, M., Goldman, M. H. S., Schwier, E. U., Braus, G. H., & Goldman, G. H. (2005) · Genetics · doi:10.1534/genetics.105.041376 · Cited by 25

The 26S Proteasome

Rechsteiner, M. (2008) · Wiley eBooks · doi:10.1002/9783527610754.dd06 · Cited by 27

The Ubiquitin-Proteasome System (UPS) as a Cancer Drug Target: Emerging Mechanisms and Therapeutics

Mata-Cantero, L., Lobato-Gil, S., Aillet, F., Lang, V., & Rodríguez, M. S. (2014) · Springer eBooks · doi:10.1007/978-94-017-9421-3_11 · Cited by 25

Plant homologue constitutive photomorphogenesis 9 (COP9) signalosome subunit CSN5 regulates innate immune responses in macrophages

Deng, Z., Pardi, R., Cheadle, W. G., Xiang, X., Zhang, S., Shah, S. V., Grizzle, W. E., Miller, D., Mountz, J. D., & Zhang, H. (2011) · Blood · doi:10.1182/blood-2010-10-314526 · Cited by 23

Resolving the CSN and CAND1 Paradoxes

Dubiel, W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.011 · Cited by 23

COPS5 inhibition arrests the proliferation and growth of serous ovarian cancer cells via the elevation of p27 level

Zhang, H., Zhong, A., Sun, J., Chen, M., Xie, S., Zheng, H., Wang, Y., Yu, Y., Guo, L., & Lu, R. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.09.070 · Cited by 23

Drosophila homolog of APP-BP1 (dAPP-BP1) interacts antagonistically with APPL during Drosophila development

Kim, H.-J., Kim, S.-H., Shim, S.-O., Park, E., Kim, C., Kim, K., Tanouye, M. A., & Yim, J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401935 · Cited by 23

Identifying Determinants of Cullin Binding Specificity Among the Three Functionally Different Drosophila melanogaster Roc Proteins via Domain Swapping

Reynolds, P. J., Simms, J. R., & Duronio, R. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002918 · Cited by 23

COPing with hypoxia

Mikus, P., & Zundel, W. (2005) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2005.03.002 · Cited by 23

The Ins(1,3,4)P3 5/6-kinase/Ins(3,4,5,6)P4 1-kinase is not a protein kinase

Qian, X., Mitchell, J. L., Wei, S., Williams, J. G., Petrovich, R. M., & Shears, S. B. (2005) · Biochemical Journal · doi:10.1042/bj20050297 · Cited by 23

The COP9 signalosome reduces neuroinflammation and attenuates ischemic neuronal stress in organotypic brain slice culture model

Tian, Y., Milic, J., Monasor, L. S., Chakraborty, R., Wang, S., Yuan, Y., Asare, Y., Behrends, C., Tahirović, S., & Bernhagen, J. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04911-8 · Cited by 22

Nanoscale coupling of endocytic pit growth and stability

Lehmann, M., Lukonin, I., Noé, F., Schmoranzer, J., Clementi, C., Loerke, D., & Haucke, V. (2019) · Science Advances · doi:10.1126/sciadv.aax5775 · Cited by 20

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

Choo, Y. Y., Boh, B. K., Lou, J. J. W., Eng, J., Leck, Y. C., Anders, B., Smith, P. G., & Hagen, T. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-03-0251 · Cited by 23

p97/ VCP promotes Cullin‐ RING ‐ubiquitin‐ligase/proteasome‐dependent degradation of IκBα and the preceding liberation of RelA from ubiquitinated IκBα

Schweitzer, K., Pralow, A., & Naumann, M. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12702 · Cited by 25

Analysis of the role of COP9 Signalosome (CSN) subunits in K562; the first link between CSN and autophagy

Pearce, C., Hayden, R. E., Bunce, C. M., & Khanim, F. L. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-31 · Cited by 22

Molecular and Neural Control of Insect Circadian Rhythms

Zhang, Y., & Emery, P. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384747-8.10015-7 · Cited by 23

RUNX3 Meets the Ubiquitin-Proteasome System in Cancer

Toska, A., Modi, N., & Chen, L. (2023) · Cells · doi:10.3390/cells12050717 · Cited by 20

Contributions of neutrophils to resolution of mucosal inflammation

Colgan, S. P., Ehrentraut, S., Glover, L. E., Kominsky, D. J., & Campbell, E. L. (2012) · Immunologic Research · doi:10.1007/s12026-012-8350-2 · Cited by 20

HIF1α-Induced by Lysophosphatidic Acid Is Stabilized via Interaction with MIF and CSN5

No, Y. R., Lee, S., Kumar, A., & Yun, C. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137513 · Cited by 20

RMP promotes epithelial-mesenchymal transition through NF-κB/CSN2/Snail pathway in hepatocellular carcinoma

Zhou, W., Wang, Q., Xu, Y., Jiang, J., Guo, J., Yu, H., & Wei, W. (2017) · Oncotarget · doi:10.18632/oncotarget.16177 · Cited by 20

Drosophila Cand1 regulates Cullin3-dependent E3 ligases by affecting the neddylation of Cullin3 and by controlling the stability of Cullin3 and adaptor protein

Kim, S., Kim, H.-J., Kim, S., & Yim, J. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.07.031 · Cited by 20

The eta7/csn3-3 Auxin Response Mutant of Arabidopsis Defines a Novel Function for the CSN3 Subunit of the COP9 Signalosome

Huang, H., Quint, M., & Gray, W. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066578 · Cited by 19

Jab1 regulates levels of endothelin type A and B receptors by promoting ubiquitination and degradation

Nishimoto, A., Lu, L., Hayashi, M., Nishiya, T., Horinouchi, T., & Miwa, S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.087 · Cited by 19

The COP9 signalosome subunit 6 (CSN6): a potential oncogene

Zhang, S.-N., Pei, D., & Zheng, J. (2013) · Cell Division · doi:10.1186/1747-1028-8-14 · Cited by 19

DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis in Arabidopsis

Mergner, J., Küster, B., & Schwechheimer, C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767103 · Cited by 19

Coupled monoubiquitylation of the co-E3 ligase DCNL1 by Ariadne-RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling

Kelsall, I. R., Kristariyanto, Y. A., Knebel, A., Wood, N. T., Kulathu, Y., & Alpi, A. F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005861 · Cited by 19

In the land of the rising sun with the COP9 signalosome and related Zomes

Pick, E., & Pintard, L. (2009) · EMBO Reports · doi:10.1038/embor.2009.27 · Cited by 19

Yeast as a tool to select inhibitors of the cullin deneddylating enzyme Csn5

Cirigliano, A., Stirpe, A., Menta, S., Mori, M., Dell’Edera, D., Pick, E., Negri, R., Botta, B., & Rinaldi, T. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2016.1160901 · Cited by 19

CSN6 aggravates Ang II-induced cardiomyocyte hypertrophy via inhibiting SIRT2

Mei, Z., Wang, H., Hu, Y., & Li, X. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112245 · Cited by 18

Molecular mechanism of the Neurospora circadian oscillator

Guo, J., & Liu, Y. (2010) · Protein & Cell · doi:10.1007/s13238-010-0053-7 · Cited by 17

Phosphorylation by COP9 Signalosome‐Associated CK2 Promotes Degradation of p27 during the G1 Cell Cycle Phase

Huang, X., Wagner, E., Dumdey, R., Peth, A., Berse, M., Dubiel, W., & Berndt, C. (2006) · Israel Journal of Chemistry · doi:10.1560/9219-25wn-yu1k-gdvv · Cited by 18

COP9 signalosome-mediated deneddylation of CULLIN1 is necessary for SCFEBF1 assembly in Arabidopsis thaliana

Dong, J., Li, Y., Cheng, S., Li, X., & Wei, N. (2024) · Cell Reports · doi:10.1016/j.celrep.2023.113638 · Cited by 16

Phytohormones in regulation of the cell division and endoreduplication process in the plant cell cycle

Tank, J. G., Pandya, R. V., & Thaker, V. S. (2014) · RSC Advances · doi:10.1039/c3ra45367g · Cited by 17

Ubiquitin-like modifiers

Taherbhoy, A. M., Schulman, B. A., & Kaiser, S. E. (2012) · Essays in Biochemistry · doi:10.1042/bse0520051 · Cited by 17

CRL4 Ubiquitin Pathway and DNA Damage Response

Zhou, P., & Fan, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_14 · Cited by 14

Coordinated Actions Between p97 and Cullin-RING Ubiquitin Ligases for Protein Degradation

Shi, W., Ding, R., Zhou, P., Fang, Y., Wan, R., Chen, Y., & Jin, J. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_5 · Cited by 17

CSN6 promotes tumorigenesis of gastric cancer by ubiquitin-independent proteasomal degradation of p16INK4a

Du, W., Liu, Z., Zhu, W.-T., Li, T., Zhu, Z., Wei, L., Song, J. H., & Pei, D. (2019) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2018.0410 · Cited by 16

Dual Regulation of Dendritic Morphogenesis in Drosophila by the COP9 Signalosome

Djagaeva, I., & Doronkin, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007577 · Cited by 16

Transcriptome analysis of auxin-regulated genes of Arabidopsis thaliana

Huang, Y.-C., Chang, Y.-L., Hsu, J.-J., & Chuang, H. (2008) · Gene · doi:10.1016/j.gene.2008.05.017 · Cited by 16

Regulation of the anaphase-promoting complex by the COP9 signalosome

Kob, R., Kelm, J., Posorski, N., Baniahmad, A., von Eggeling, F., & Melle, C. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8850 · Cited by 16

COP9 SIGNALOSOME SUBUNIT 5A facilitates POLYAMINE OXIDASE 5 degradation to regulate strawberry plant growth and fruit ripening

Huang, Y., Gao, J., Ji, G., Li, W., Wang, J., Wang, Q., Shen, Y., Guo, J., & Gao, F. (2025) · The Plant Cell · doi:10.1093/plcell/koaf022 · Cited by 15

PAN-1, a P-granule component important for C. elegans fertility, has dual roles in the germline and soma

Gao, G., Deeb, F., Mercurio, J. M., Parfenova, A., Smith, P. A., & Bennett, K. L. (2012) · Developmental Biology · doi:10.1016/j.ydbio.2012.02.006 · Cited by 15

SMALL ACIDIC PROTEIN1 Acts with RUB Modification Components, the COP9 Signalosome, and AXR1 to Regulate Growth and Development of Arabidopsis

Nakasone, A., Fujiwara, M., Fukao, Y., Biswas, K. K., Rahman, A., Kawai‐Yamada, M., Narumi, I., Uchimiya, H., & Oono, Y. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.188409 · Cited by 15

An overactive neddylation pathway serves as a therapeutic target and MLN4924 enhances the anticancer activity of cisplatin in pancreatic cancer

Zeng, Y., Iv, Y., Pan, Q., Zhou, Y., & He, L. (2019) · Oncology Letters · doi:10.3892/ol.2019.10596 · Cited by 15

G Protein Pathway Suppressor 1 Promotes Influenza Virus Polymerase Activity by Activating the NF-κB Signaling Pathway

Kuwahara, T., Yamayoshi, S., Noda, T., & Kawaoka, Y. (2019) · mBio · doi:10.1128/mbio.02867-19 · Cited by 15

Regulation of T cell receptor complex-mediated signaling by ubiquitin and ubiquitin-like modifications

Friend, S. F., Deason-Towne, F., Peterson, L. K., Berger, A., & Dragone, L. L. (2014) · Europe PMC (PubMed Central) · doi:10.25677/gwxq-0d13 · Cited by 15

In Vitro Cleavage of Nedd8 from Cullin 1 by COP9 Signalosome and Deneddylase 1

Yamoah, K., Wu, K. K.-Y., & Pan, Z. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)98042-7 · Cited by 15

PEA15 Regulates the DNA Damage-Induced Cell Cycle Checkpoint and Oncogene-Directed Transformation

Nagarajan, A. G., Dogra, S. K., Liu, A. Y., Green, M. R., & Wajapeyee, N. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01542-13 · Cited by 15

Prospect of divergent roles for the CUL3 system in vascular endothelial cell function and angiogenesis

Sakaue, T., Maekawa, M., Nakayama, H., & Higashiyama, S. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx051 · Cited by 14

Proteome profile of neutrophils from a transgenic diabetic pig model shows distinct changes

Weigand, M., Degroote, R. L., Amann, B., Renner, S., Wolf, E., Hauck, S. M., & Deeg, C. A. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103843 · Cited by 14

Neddylation and CAND1 Independently Stimulate SCF Ubiquitin Ligase Activity in Candida albicans

Sela, N., Atir-Lande, A., & Kornitzer, D. (2011) · Eukaryotic Cell · doi:10.1128/ec.05250-11 · 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

Electron microscopy and in vitro deneddylation reveal similar architectures and biochemistry of isolated human and Flag-mouse COP9 signalosome complexes

Rockel, B., Schmaler, T., Huang, X., & Dubiel, W. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.06.093 · Cited by 13

Deregulation of the COP9 signalosome–cullin-RING ubiquitin-ligase pathway: Mechanisms and roles in urological cancers

Gummlich, L., Rabien, A., Jung, K., & Dubiel, W. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.03.023 · Cited by 15

CSN5 controls the growth of osteosarcoma via modulating the EGFR/PI3K/Akt axis

Wan, Z., Huang, S., Mo, F., Yao, Y., Liu, G., Han, Z., Chen, M., & Li, Z. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111646 · 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

The Antioxidant Enzyme Methionine Sulfoxide Reductase A (MsrA) Interacts with Jab1/CSN5 and Regulates Its Function

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Life Is Degrading—Thanks to Some Zomes

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COP9 signalosome subunit 6 mediates PDGF -induced pulmonary arterial smooth muscle cells proliferation

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Depletion of CSN5 inhibits Ras‐mediated tumorigenesis by inducing premature senescence in p53‐null cells

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

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