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

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

THE UBIQUITIN SYSTEM

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

Mechanisms Underlying Ubiquitination

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

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

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

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

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

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

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

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767

Advancing targeted protein degradation for cancer therapy

Dale, B., Cheng, M., Park, K., Kanıskan, H. Ü., Xiong, Y., & Jin, J. J. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00365-x · Cited by 697

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 cullin protein family

Sarikas, A., Hartmann, T., & Pan, Z. (2011) · Genome biology · doi:10.1186/gb-2011-12-4-220 · Cited by 541

The Cullin-RING Ubiquitin-Protein Ligases

Hua, Z., & Vierstra, R. D. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112256 · Cited by 523

Ubiquitin, Hormones and Biotic Stress in Plants

Dreher, K. A., & Callis, J. (2007) · Annals of Botany · doi:10.1093/aob/mcl255 · Cited by 512

The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation

Fischer, E. S., Scrima, A., Böhm, K., Matsumoto, S., Lingaraju, G. M., Faty, M., Yasuda, T., Cavadini, S., Wakasugi, M., Hanaoka, F., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.035 · Cited by 460

The ubiquitin‐proteasome system regulates plant hormone signaling

Santner, A. A., & Estelle, M. A. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04112.x · Cited by 434

Multimodal Activation of the Ubiquitin Ligase SCF by Nedd8 Conjugation

Saha, A., & Deshaies, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.021 · Cited by 401

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

Function and regulation of protein neddylation

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

Keap1, the cysteine-based mammalian intracellular sensor for electrophiles and oxidants

Dinkova‐Kostova, A. T., Kostov, R. V., & Canning, P. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.005 · Cited by 340

DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4–ROC1 ubiquitin ligasesPreprint

He, Y. J., McCall, C. M., Hu, J., Zeng, Y., & Xiong, Y. (2006) · Genes & Development · doi:10.1101/gad.1483206 · Cited by 338

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

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

Cullin-RING Ligases as Attractive Anti-cancer Targets

Zhao, Y., & Sun, Y. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990300 · Cited by 279

NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly

Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020) · Nature · doi:10.1038/s41586-020-2000-y · Cited by 270

The ubiquitin proteasome system — Implications for cell cycle control and the targeted treatment of cancer

Bassermann, F. C., Eichner, R., & Pagano, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.028 · Cited by 278

Structural Mechanisms Underlying Posttranslational Modification by Ubiquitin-Like Proteins

Dye, B. T., & Schulman, B. A. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132820 · Cited by 272

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

Cullin-RING Ubiquitin Ligase Regulatory Circuits: A Quarter Century Beyond the F-Box Hypothesis

Harper, J. W., & Schulman, B. A. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090120-013613 · Cited by 262

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

Structure of hsDDB1-drDDB2 bound to a 13 bp CPD-duplex (purine at D-1 position) at 3.0 A resolution (CPD 1)

Scrima, A., Fischer, E. S., Iwai, S., Gut, H., & Thomä, N. H. (2011) · Worldwide Protein Data Bank · doi:10.2210/pdb4a08/pdb · Cited by 233

Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats

Sibanda, B. L., Chirgadze, D. Y., & Blundell, T. L. (2009) · Nature · doi:10.1038/nature08648 · Cited by 225

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

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 basis for autoinhibition and phosphorylation-dependent activation of c-Cbl

Dou, H., Buetow, L., Hock, A., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2231 · Cited by 216

Structural regulation of cullin-RING ubiquitin ligase complexes

Duda, D. M., Scott, D. C., Calabrese, M. F., Zimmerman, E. S., Zheng, N., & Schulman, B. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.01.003 · Cited by 205

Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation

Kurz, T., Chou, Y.-C., Willems, A. R., Meyer‐Schaller, N., Hecht, M.-L., Tyers, M., Peter, M., & Sicheri, F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.012 · Cited by 200

Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8

Scott, D. C., Sviderskiy, V. O., Monda, J. K., Lydeard, J. R., Cho, S. E., Harper, J. W., & Schulman, B. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.037 · Cited by 201

Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment

Li, W., Li, F., Zhang, X., Lin, H., & Xu, C. S. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00825-8 · Cited by 211

Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization

Merlet, J., Burger, J., Gomes, J., & Pintard, L. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8712-7 · Cited by 203

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

Protein–protein interaction through β-strand addition

Remaut, H. K., & Waksman, G. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.06.007 · Cited by 199

The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle

Schmidt, M., Haas, W., Crosas, B., Santamarı́a, P. G., Gygi, S. P., Walz, T., & Finley, D. J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb914 · Cited by 184

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

Auxin Perception--Structural Insights

Calderon-Villalobos, L. I., Tan, X., Zheng, N., & Estelle, M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005546 · Cited by 177

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

Protein neddylation and its role in health and diseases

Zhang, S., Yu, Q., Li, Z., Zhao, Y., & Sun, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01800-9 · Cited by 171

Radiosensitization of Human Pancreatic Cancer Cells by MLN4924, an Investigational NEDD8-Activating Enzyme Inhibitor

Wei, D., Li, H., Yu, J., Sebolt, J. T., Zhao, L., Lawrence, T. S., Smith, P. G., Morgan, M. A., & Sun, Y. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-2866 · Cited by 169

Structural and Functional Insights to Ubiquitin-Like Protein Conjugation

Streich, F. C., & Lima, C. D. (2014) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-051013-022958 · Cited by 176

Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 Forms a Nuclear E3 Ubiquitin Ligase with DDB1 and CUL4 That Is Involved in Multiple Plant Developmental Processes

Zhang, Y., Feng, S., Chen, F., Chen, H., Wang, J., McCall, C. M., Xiong, Y., & Deng, X. W. (2008) · The Plant Cell · doi:10.1105/tpc.108.058891 · Cited by 168

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

Induction of p21-Dependent Senescence by an NAE Inhibitor, MLN4924, as a Mechanism of Growth Suppression

Jia, L., Li, H., & Sun, Y. (2011) · Neoplasia · doi:10.1593/neo.11420 · Cited by 155

Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex

Cardote, T. A. F., Gadd, M. S., & Ciulli, A. (2017) · Structure · doi:10.1016/j.str.2017.04.009 · Cited by 150

Control of cell growth by the SCF and APC/C ubiquitin ligases

Skaar, J. R., & Pagano, M. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.08.004 · Cited by 159

SCF E3 Ubiquitin Ligases as Anticancer Targets

Jia, L., & Sun, Y. (2011) · Current Cancer Drug Targets · doi:10.2174/156800911794519734 · Cited by 147

PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis

Grinthal, A., Adamovic, I., Weiner, B. M., Karplus, M., & Kleckner, N. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914073107 · Cited by 139

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

Structural and functional coupling of Hsp90‐ and Sgt1‐centred multi‐protein complexes

Zhang, M., Botër, M., Li, K., Kadota, Y., Panaretou, B., Prodromou, C., Shirasu, K., & Pearl, L. H. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.190 · Cited by 130

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

Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1

Shen, L., Liu, H., Dong, C., Xirodimas, D. P., Naismith, J. H., & Hay, R. T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600628 · Cited by 119

Deconjugation of Nedd8 from Cul1 Is Directly Regulated by Skp1-F-box and Substrate, and the COP9 Signalosome Inhibits Deneddylated SCF by a Noncatalytic Mechanism

Emberley, E. D., Mosadeghi, R., & Deshaies, R. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.352484 · Cited by 118

Genetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases

Zhou, W., Wei, W., & Sun, Y. (2013) · Cell Research · doi:10.1038/cr.2013.44 · Cited by 114

Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B

Hannah, J., & Zhou, P. (2015) · Gene · doi:10.1016/j.gene.2015.08.064 · Cited by 112

Cand1-Mediated Adaptive Exchange Mechanism Enables Variation in F-Box Protein Expression

Liu, X., Reitsma, J. M., Mamrosh, J. L., Zhang, Y., Straube, R., & Deshaies, R. J. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.038 · Cited by 108

Expression and Characterization of Full-length Human Huntingtin, an Elongated HEAT Repeat Protein

Li, W., Serpell, L. C., Carter, W. J., Rubinsztein, D. C., & Huntington, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511007200 · Cited by 106

A Dual E3 Mechanism for Rub1 Ligation to Cdc53

Scott, D. C., Monda, J. K., Grace, C. R., Duda, D. M., Kriwacki, R. W., Kurz, T., & Schulman, B. A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.030 · Cited by 102

Characterisation of the Cullin‐3 mutation that causes a severe form of familial hypertension and hyperkalaemia

Schumacher, F., Siew, K., Zhang, J., Johnson, C., Wood, N. T., Cleary, S. E., Maskari, R. A., Ferryman, J. T., Hardege, I., Yasmin, Y., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505444 · Cited by 104

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

Lo, S., & Hannink, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1235-1244.2006 · Cited by 99

Small RING Finger Proteins RBX1 and RBX2 of SCF E3 Ubiquitin Ligases: The Role in Cancer and as Cancer Targets

Wei, D., & Sun, Y. (2010) · Genes & Cancer · doi:10.1177/1947601910382776 · Cited by 98

Functional analysis of EID1, an F‐box protein involved in phytochrome A‐dependent light signal transduction

Marrocco, K., Zhou, Y., Bury, E., Dieterle, M., Funk, M., Genschik, P., Krenz, M., Stolpe, T., & Kretsch, T. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2005.02635.x · Cited by 95

SCCRO (DCUN1D1) Is an Essential Component of the E3 Complex for Neddylation

Kim, A. Y., Bommeljé, C. C., Lee, B. E., Yonekawa, Y., Choi, L., Morris, L. G. T., Huang, G., Kaufman, A., Ryan, R. J. H., Hao, B., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804440200 · Cited by 93

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

The p21-Dependent Radiosensitization of Human Breast Cancer Cells by MLN4924, an Investigational Inhibitor of NEDD8 Activating Enzyme

Yang, D., Tan, M., Wang, G., & Sun, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034079 · Cited by 94

AhSSK1, a novel SKP1‐like protein that interacts with the S‐locus F‐box protein SLF

Huang, J. H., Zhao, L., Yang, Q., & Xue, Y. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02735.x · Cited by 95

Substrate-mediated Regulation of Cullin Neddylation

Chew, E., & Hagen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701153200 · Cited by 91

The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at membranes

Meyer‐Schaller, N., Chou, Y.-C., Sumara, I., Martin, D. D. O., Kurz, T., Katheder, N. S., Hofmann, K., Berthiaume, L. G., Sicheri, F., & Peter, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812528106 · Cited by 91

Control of Cullin-Ring Ubiquitin Ligase Activity by Nedd8

Deshaies, R. J., Emberley, E. D., & Saha, A. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_4 · Cited by 91

Structure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding Surface

Duda, D. M., Olszewski, J. L., Tron, A. E., Hammel, M., Lambert, L. J., Waddell, M. B., Mittag, T., DeCaprio, J. A., & Schulman, B. A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.044 · Cited by 93

NEDD8 — its role in the regulation of Cullin-RING ligases

Schwechheimer, C. (2018) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2018.05.017 · Cited by 84

Characterization of a novel temperature‐sensitive allele of the CUL1/AXR6 subunit of SCF ubiquitin‐ligases

Quint, M., Ito, H., Zhang, W., & Gray, W. M. (2005) · The Plant Journal · doi:10.1111/j.1365-313x.2005.02449.x · Cited by 88

The ROQ domain of Roquin recognizes mRNA constitutive-decay element and double-stranded RNA

Tan, D., Zhou, M., Kiledjian, M., & Tong, L. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2857 · Cited by 86

HSP90 functions in the circadian clock through stabilization of the client F-box protein ZEITLUPE

Kim, T.-S., Kim, W. Y., Fujiwara, S., Kim, J., Cha, J., Park, J., Lee, S. Y., & Somers, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110406108 · Cited by 84

HSP 90s are required for NLR immune receptor accumulation in Arabidopsis

Huang, S., Monaghan, J., Zhong, X., Lin, L., Sun, T., Dong, O. X., & Li, X. (2014) · The Plant Journal · doi:10.1111/tpj.12573 · Cited by 85

A New CULLIN 1 Mutant Has Altered Responses to Hormones and Light in Arabidopsis

Moon, J., Zhao, Y., Dai, X., Zhang, W., Gray, W. M., Huq, E., & Estelle, M. A. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.091439 · Cited by 87

Targeting BIG3–PHB2 interaction to overcome tamoxifen resistance in breast cancer cells

Yoshimaru, T., Komatsu, M., Matsuo, T., Chen, Y., Murakami, Y., Mizuguchi, K., Mizohata, E., Tsuyoshi Inoue, A., Akiyama, M. O., Yamaguchi, R., et al. (2013) · Nature Communications · doi:10.1038/ncomms3443 · Cited by 78

Cullins and Cancer

Lee, J., & Zhou, P. (2010) · Genes & Cancer · doi:10.1177/1947601910382899 · Cited by 84

Plant TRAF Proteins Regulate NLR Immune Receptor Turnover

Huang, S., Chen, X., Zhong, X., Li, M., Ao, K., Huang, J., & Li, X. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.01.005 · Cited by 78

ALKBH5/YTHDF2‐mediated m6A modification of circAFF2 enhances radiosensitivity of colorectal cancer by inhibiting Cullin neddylation

Shao, Y., Liu, Z., Song, X., Sun, R., Zhou, Y., Zhang, D., Sun, H., Huang, J., Wu, C., Gu, W., et al. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1318 · Cited by 78

Cryo-EM Structure of the DNA-Dependent Protein Kinase Catalytic Subunit at Subnanometer Resolution Reveals α Helices and Insight into DNA Binding

Williams, D., Lee, K. J., Shi, J. R., Chen, D. J., & Stewart, P. L. (2008) · Structure · doi:10.1016/j.str.2007.12.014 · Cited by 81

Development of inhibitors in the ubiquitination cascade

Zhang, W., & Sidhu, S. S. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.003 · Cited by 77

Degrade to create: developmental requirements for ubiquitin-mediated proteolysis during earlyC. elegansembryogenesis

Bowerman, B. A., & Kurz, T. (2006) · Development · doi:10.1242/dev.02276 · Cited by 77

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Structural Insight into the Assembly of TRPV Channels

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COP9 Signalosome- and 26S Proteasome-dependent Regulation of SCFTIR1 Accumulation in Arabidopsis

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Protection of cullin–RING E3 ligases by CSN–UBP12

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Composition, Roles, and Regulation of Cullin-Based Ubiquitin E3 Ligases

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Assembly and Regulation of CRL Ubiquitin Ligases

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Inhibition of NEDD8‐conjugation pathway by novel molecules: Potential approaches to anticancer therapy

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CAND1 Binds to Unneddylated CUL1 and Regulates the Formation of SCF Ubiquitin E3 Ligase Complex

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Structural and mechanistic insights into the CAND1-mediated SCF substrate receptor exchange

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NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases

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Sequential Processivity and CAND1 Regulate SCF Ubiquitin Ligases

Pierce, N. W. (2012) · CaltechTHESIS (California Institute of Technology) · doi:10.7907/me1h-ak32