The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications

Cancer Metastasis: Building a Framework

Gupta, G. P., & Massagué, J. (2006) · Cell · doi:10.1016/j.cell.2006.11.001 · Cited by 4,230 · see citing works

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 · see citing works

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 · see citing works

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

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

The Arabidopsis NPR1 Gene That Controls Systemic Acquired Resistance Encodes a Novel Protein Containing Ankyrin Repeats

Cao, H., Glazebrook, J., Clarke, J. D., Volko, S. M., & Dong, X. (1997) · Cell · doi:10.1016/s0092-8674(00)81858-9 · Cited by 1,572 · see citing works

Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution

Taguchi, K., Motohashi, H., & Yamamoto, M. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01473.x · Cited by 1,478 · see citing works

THE UBIQUITIN 26S PROTEASOME PROTEOLYTIC PATHWAY

Smalle, J., & Vierstra, R. D. (2004) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.55.031903.141801 · Cited by 1,350 · see citing works

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 1,262 · see citing works

Dysfunctional KEAP1–NRF2 Interaction in Non-Small-Cell Lung Cancer

Singh, A., Misra, V., Thimmulappa, R. K., Lee, H., Ames, S., Hoque, M. O., Herman, J. G., Baylin, S. B., Sidransky, D., Gabrielson, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030420 · Cited by 1,060 · see citing works

Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers

Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986 · see citing works

The Keap1-BTB Protein Is an Adaptor That Bridges Nrf2 to a Cul3-Based E3 Ligase: Oxidative Stress Sensing by a Cul3-Keap1 Ligase

Cullinan, S. B., Gordan, J. D., Jin, J., Harper, J. W., & Diehl, J. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8477-8486.2004 · Cited by 986 · see citing works

NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants

Fu, Z. Q., Yan, S., Saleh, A., Wang, W., Ruble, J., Oka, N., Mohan, R., Spoel, S. H., Tada, Y., Zheng, N., et al. (2012) · Nature · doi:10.1038/nature11162 · Cited by 978 · see citing works

Recent advances and emerging trends in plant hormone signalling

Santner, A., & Estelle, M. (2009) · Nature · doi:10.1038/nature08122 · Cited by 960 · see citing works

Role of VHL Gene Mutation in Human Cancer

Kim, W. Y., & Kaelin, W. G. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.05.061 · Cited by 940 · see citing works

Ubiquitin-mediated proteolysis: biological regulation via destruction

Ciechanover, A. J., Orian, A., & Schwartz, A. L. (2000) · BioEssays · doi:10.1002/(sici)1521-1878(200005)22:5 · Cited by 845 · see citing works

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 · see citing works

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · cited 1× · see citing works

Cancer related mutations in <i>NRF2</i> impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy

Shibata, T., Ohta, T., Tong, K. I., Kokubu, A., Odogawa, R., Tsuta, K., Asamura, H., Yamamoto, M., & Hirohashi, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806268105 · Cited by 728 · see citing works

Systematic analysis and nomenclature of mammalian F-box proteinsPreprint

Jin, J., Cardozo, T. J., Lovering, R. C., Elledge, S. J., Pagano, M., & Harper, J. W. (2004) · Genes & Development · doi:10.1101/gad.1255304 · Cited by 716 · see citing works

The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis

Gagne, J. M., Downes, B. P., Shiu, S., Durski, A. M., & Vierstra, R. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162339999 · Cited by 695 · see citing works

Sequence and structural analysis of BTB domain proteins

Stogios, P. J., Downs, G. S., Jauhal, J. J., Nandra, S. K., & Privé, G. G. (2005) · Genome Biology · doi:10.1186/gb-2005-6-10-r82 · Cited by 694 · see citing works

Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities

Boyden, L. M., Choi, M., Choate, K. A., Nelson-Williams, C. J., Farhi, A., Toka, H. R., Tikhonova, I. R., Bjornson, R. D., Mane, S., Colussi, G., et al. (2012) · Nature · doi:10.1038/nature10814 · Cited by 641 · see citing works

Loss of Keap1 Function Activates Nrf2 and Provides Advantages for Lung Cancer Cell Growth

Ohta, T., Iijima, K., Miyamoto, M., Nakahara, I., Tanaka, H., Ohtsuji, M., Suzuki, T., Kobayashi, A., Yokota, J., Sakiyama, T., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5003 · Cited by 630 · see citing works

Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604 · see citing works

Proteasome-Mediated Turnover of the Transcription Coactivator NPR1 Plays Dual Roles in Regulating Plant Immunity

Spoel, S. H., Mou, Z., Tada, Y., Spivey, N. W., Genschik, P., & Dong, X. (2009) · Cell · doi:10.1016/j.cell.2009.03.038 · Cited by 603 · see citing works

Cullin3-Based Polyubiquitination and p62-Dependent Aggregation of Caspase-8 Mediate Extrinsic Apoptosis Signaling

Jin, Z., Li, Y., Pitti, R. M., Lawrence, D. A., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 588 · see citing works

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 509 · see citing works

BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

Xu, L., Yue, W., Reboul, J., Vaglio, P., Shin, T.-H., Vidal, M., Elledge, S. J., & Harper, J. W. (2003) · Nature · doi:10.1038/nature01985 · Cited by 497 · see citing works

Dimerization of Substrate Adaptors Can Facilitate Cullin-mediated Ubiquitylation of Proteins by a “Tethering” Mechanism

McMahon, M. J., Thomas, N., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601119200 · Cited by 489 · see citing works

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases

Zhuang, M., Calabrese, M. F., Liu, J., Waddell, M. B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.022 · Cited by 486 · see citing works

Targeting of protein ubiquitination by BTB–Cullin 3–Roc1 ubiquitin ligases

Furukawa, M., He, Y. J., Borchers, C. H., & Xiong, Y. (2003) · Nature Cell Biology · doi:10.1038/ncb1056 · Cited by 459 · see citing works

The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

Pintard, L., Willis, J. H., Willems, A. R., Johnson, J.-L., Srayko, M., Kurz, T., Luke-Glaser, S., Mains, P. E., Tyers, M., Bowerman, B. A., et al. (2003) · Nature · doi:10.1038/nature01959 · Cited by 431 · see citing works

Cullin‐based ubiquitin ligases: Cul3–BTB complexes join the family

Pintard, L., Willems, A. R., & Peter, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600186 · Cited by 413 · see citing works

The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy

Bomont, P., Cavalier, L., Blondeau, F., Hamida, C. B., Belal, S., Tazir, M., Demir, E., Topaloğlu, H., Korinthenberg, R., Tüysüz, B., et al. (2000) · Nature Genetics · doi:10.1038/81701 · Cited by 408 · see citing works

Molecular pathogenesis of inherited hypertension with hyperkalemia: The Na–Cl cotransporter is inhibited by wild-type but not mutant WNK4

Wilson, F. H., Kahle, K. T., Sabath, E., Lalioti, M. D., Rapson, A. K., Hoover, R. S., Hébert, S., Gamba, G., & Lifton, R. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242735399 · Cited by 405 · see citing works

Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cellsPreprint

Singer, J. D., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.18.2375 · Cited by 404 · see citing works

Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 protein

Wang, K. L.-C., Yoshida, H., Claire Lurin, A., & Ecker, J. R. (2004) · Nature · doi:10.1038/nature02516 · Cited by 399 · see citing works

KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ

Lee, D.-F., Kuo, H.-P., Liu, M., Chou, C.-K., Xia, W., Du, Y., Shen, J., Chen, C.-T., Huo, L., Hsu, M.-C., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.025 · Cited by 399 · see citing works

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 396 · see citing works

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 386 · see citing works

The eto1 , eto2 , and eto3 Mutations and Cytokinin Treatment Increase Ethylene Biosynthesis in Arabidopsis by Increasing the Stability of ACS Protein

Chae, H. S., Faure, F., & Kieber, J. J. (2003) · The Plant Cell · doi:10.1105/tpc.006882 · Cited by 379 · see citing works

The KLHL12–Cullin-3 ubiquitin ligase negatively regulates the Wnt–β-catenin pathway by targeting Dishevelled for degradation

Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364 · see citing works

Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1 and regulates hormone responses in Arabidopsis

Himmelbach, A., Hoffmann, T., Leube, M., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf316 · Cited by 362 · see citing works

Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conservedPreprint

Chen, M.-H., Wilson, C. W., Li, Y.-J., Law, K. K. L., Lu, C.-S., Gacayan, R., Zhang, X., Hui, C., & Chuang, P. (2009) · Genes & Development · doi:10.1101/gad.1794109 · Cited by 353 · see citing works

The role of ubiquitylation in immune defence and pathogen evasion

Jiang, X., & Chen, Z. J. (2011) · Nature reviews. Immunology · doi:10.1038/nri3111 · Cited by 350 · see citing works

BTB/POZ Domain Proteins Are Putative Substrate Adaptors for Cullin 3 Ubiquitin Ligases

Geyer, R. K., Wee, S., Anderson, S., Yates, J. R., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00341-1 · Cited by 339 · see citing works

KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron

Louis-Dit-Picard, H., Barc, J., Trujillano, D., Miserey‐Lenkei, S., Bouatia‐Naji, N., Pylypenko, O., Beaurain, G., Bonnefond, A., Sand, O., Simian, C., et al. (2012) · Nature Genetics · doi:10.1038/ng.2218 · Cited by 337 · see citing works

Ubiquitin-dependent regulation of COPII coat size and function

Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Baumgärtel, C., Schekman, R., & Rape, M. (2012) · Nature · doi:10.1038/nature10822 · Cited by 330 · see citing works

<i>Arabidopsis</i> NPH3: A NPH1 Photoreceptor-Interacting Protein Essential for Phototropism

Motchoulski, A., & Liscum, E. (1999) · Science · doi:10.1126/science.286.5441.961 · Cited by 320 · see citing works

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

Liu, J., Furukawa, M., Matsumoto, T., & Xiong, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00783-9 · Cited by 319 · see citing works

Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase

Hernández‐Muñoz, I., Lund, A. H., van der Stoop, P. P. M., Boutsma, E., Muijrers, I., Verhoeven, E., Nusinow, D. A., Panning, B., Marahrens, Y., & van Lohuizen, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408918102 · Cited by 312 · see citing works

Crystal structure of the BTB domain from PLZF

Ahmad, K. F., Engel, C. K., & Privé, G. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12123 · Cited by 296 · see citing works

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284 · see citing works

Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement

Chen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Ding, M., Peng, H. B., & Shao, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.004 · Cited by 270 · see citing works

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

Scott, D. C., Monda, J. K., Bennett, E. J., Harper, J. W., & Schulman, B. A. (2011) · Science · doi:10.1126/science.1209307 · Cited by 270 · see citing works

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 · see citing works

Plant stomata: a checkpoint of host immunity and pathogen virulence

Zeng, W., Melotto, M., & He, S. Y. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.05.006 · Cited by 255 · see citing works

Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4

Shibata, S., Zhang, J., Puthumana, J., Stone, K. L., & Lifton, R. P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304592110 · Cited by 253 · see citing works

RPT2: A Signal Transducer of the Phototropic Response in Arabidopsis

Sakai, T., Wada, T., Ishiguro, S., & Okada, K. (2000) · The Plant Cell · doi:10.1105/tpc.12.2.225 · Cited by 253 · see citing works

A Cul3-Based E3 Ligase Removes Aurora B from Mitotic Chromosomes, Regulating Mitotic Progression and Completion of Cytokinesis in Human Cells

Sumara, I., Quadroni, M., Frei, C., Olma, M. H., Sumara, G., Ricci, R., & Peter, M. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.019 · Cited by 230 · see citing works

A Hedgehog-Induced BTB Protein Modulates Hedgehog Signaling by Degrading Ci/Gli Transcription Factor

Zhang, Q. H., Zhang, L., Wang, B., Ou, C.-Y., Chien, C., & Jiang, J. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.05.004 · Cited by 225 · see citing works

The CUL3–KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction

Ohta, A., Schumacher, F., Mehellou, Y., Johnson, C., Knebel, A., Macartney, T., Wood, N. T., Alessi, D. R., & Kurz, T. (2013) · Biochemical Journal · doi:10.1042/bj20121903 · Cited by 223 · see citing works

Suppression of NF-κB signaling by KEAP1 regulation of IKKβ activity through autophagic degradation and inhibition of phosphorylation

Kim, J.-E., You, D., Lee, C., Ahn, C., Seong, J. Y., & Hwang, J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.06.004 · Cited by 223 · see citing works

Impaired KLHL3-Mediated Ubiquitination of WNK4 Causes Human Hypertension

Wakabayashi, M., Mori, T., Isobe, K., Sohara, E., Susa, K., Araki, Y., Chiga, M., Kikuchi, E., Nomura, N., Mori, Y., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.024 · Cited by 216 · see citing works

Identification of SCF Ubiquitin Ligase Substrates by Global Protein Stability Profiling

Yen, H.-C. S., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1160462 · Cited by 209 · see citing works

BTB Domain-containing Speckle-type POZ Protein (SPOP) Serves as an Adaptor of Daxx for Ubiquitination by Cul3-based Ubiquitin Ligase

Kwon, J. E., La, M., Oh, K. H., Oh, Y. M., Ryang, K. G., Seol, J. H., Baek, S. H., Chiba, T., Tanaka, K., Bang, O. S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600204200 · Cited by 206 · see citing works

Cytoskeletal Regulation by the Nedd8 Ubiquitin-Like Protein Modification Pathway

Kurz, T., Pintard, L., Willis, J. H., Hamill, D. R., Gönczy, P., Peter, M., & Bowerman, B. A. (2002) · Science · doi:10.1126/science.1067765 · Cited by 204 · see citing works

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 197 · see citing works

Naming a targeting signal

Varshavsky, A. J. (1991) · Cell · doi:10.1016/0092-8674(91)90202-a · Cited by 195 · see citing works

A Cullin3-KLHL20 Ubiquitin Ligase-Dependent Pathway Targets PML to Potentiate HIF-1 Signaling and Prostate Cancer Progression

Yuan, W.-C., Lee, Y.-R., Huang, S.-F. K., Lin, Y., Chen, T.-Y., Chung, H.-C., Tsai, C.-H., Chen, H., Chiang, C.-T., Lai, C.-K., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.07.008 · Cited by 186 · see citing works

Translational Homeostasis via the mRNA Cap-Binding Protein, eIF4E

Yanagiya, A., Suyama, E., Adachi, H., Svitkin, Y. V., Aza‐Blanc, P., Imataka, H., Mikami, S., Martineau, Y., Ronai, Z. A., & Sonenberg, N. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.004 · Cited by 182 · see citing works

Arabidopsis Has Two Redundant Cullin3 Proteins That Are Essential for Embryo Development and That Interact with RBX1 and BTB Proteins to Form Multisubunit E3 Ubiquitin Ligase Complexes in Vivo

Figueroa, P. M., Gusmaroli, G., Serino, G., Habashi, J., Ma, L., Shen, Y., Feng, S., Bostick, M. L., Callis, J., Hellmann, H. A., et al. (2005) · The Plant Cell · doi:10.1105/tpc.105.031989 · Cited by 182 · see citing works

The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidopsis by controlling type‐2 ACC synthase levels

Christians, M. J., Gingerich, D. J., Hansen, M., Binder, B. M., Kieber, J. J., & Vierstra, R. D. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03693.x · Cited by 180 · see citing works

Cullins 3a and 3b Assemble with Members of the Broad Complex/Tramtrack/Bric-a-Brac (BTB) Protein Family to Form Essential Ubiquitin-Protein Ligases (E3s) in Arabidopsis

Gingerich, D. J., Gagne, J. M., Salter, D. W., Hellmann, H. A., Estelle, M. A., Ma, L., & Vierstra, R. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413247200 · Cited by 179 · see citing works

Neddylation and Deneddylation of CUL-3 Is Required to Target MEI-1/Katanin for Degradation at the Meiosis-to-Mitosis Transition in C. elegans

Pintard, L., Kurz, T., Luke-Glaser, S., Willis, J. H., Peter, M., & Bowerman, B. A. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00336-1 · Cited by 178 · see citing works

Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1

Li, C., Ao, J., Fu, J., Lee, D.-F., Xu, J., Lonard, D. M., & O’Malley, B. W. (2011) · Oncogene · doi:10.1038/onc.2011.151 · Cited by 173 · see citing works

Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3

Pedmale, U. V., & Liscum, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702551200 · Cited by 169 · see citing works

MATH/BTB CRL3 Receptors Target the Homeodomain-Leucine Zipper ATHB6 to Modulate Abscisic Acid Signaling

Lechner, E., Leonhardt, N., Eisler, H., Parmentier, Y., Alioua, M., Jacquet, H., Leung, J., & Genschik, P. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.018 · Cited by 168 · see citing works

TRAF2 Sets a Threshold for Extrinsic Apoptosis by Tagging Caspase-8 with a Ubiquitin Shutoff Timer

Gonzalvez, F., Lawrence, D., Yang, B., Yee, S. F., Pitti, R. M., Marsters, S. A., Pham, V. C., Stéphan, J.-P., Lill, J. R., & Ashkenazi, A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.031 · Cited by 163 · see citing works

Adaptive evolution in two large families of ubiquitin-ligase adapters in nematodes and plantsPreprint

Thomas, J. H. (2006) · Genome Research · doi:10.1101/gr.5089806 · Cited by 163 · see citing works

Dominant Mutations in KBTBD13, a Member of the BTB/Kelch Family, Cause Nemaline Myopathy with Cores

Sambuughin, N., Yau, K. S., Olivé, M., Duff, R. M., Bayarsaikhan, M., Lu, S., González, L., Sivadorai, P., Nowak, K. J., Ravenscroft, G., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.10.020 · Cited by 163 · see citing works

NF-κB activation in cancer: a challenge for ubiquitination- and proteasome-based therapeutic approach

Amit, S., & Ben‐Neriah, Y. (2003) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00096-2 · Cited by 152 · see citing works

Modulation of Phototropic Responsiveness in <i>Arabidopsis</i> through Ubiquitination of Phototropin 1 by the CUL3-Ring E3 Ubiquitin Ligase CRL3NPH3

Roberts, D., Pedmale, U. V., Morrow, J., Sachdev, S., Lechner, E., Tang, X., Zheng, N., Hannink, M., Genschik, P., & Liscum, E. (2011) · The Plant Cell · doi:10.1105/tpc.111.087999 · Cited by 150 · see citing works

Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase

Zhang, Q., Shi, Q., Chen, Y., Yue, T., Li, S., Wang, B., & Jiang, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912008106 · Cited by 149 · see citing works

Protein Phosphatase 2A Controls Ethylene Biosynthesis by Differentially Regulating the Turnover of ACC Synthase Isoforms

Skottke, K. R., Yoon, G. M., Kieber, J. J., & DeLong, A. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001370 · Cited by 146 · see citing works

Arabidopsis AtCUL3a and AtCUL3b Form Complexes with Members of the BTB/POZ-MATH Protein Family

Weber, H., Bernhardt, A., Dieterle, M., Hano, P., Mutlu, A., Estelle, M. A., Genschik, P., & Hellmann, H. A. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.052654 · Cited by 145 · see citing works

Adaptor Protein Self-Assembly Drives the Control of a Cullin-RING Ubiquitin Ligase

Errington, W. J., Khan, M. Q., Bueler, S. A., Rubinstein, J. L., Chakrabartty, A., & Privé, G. G. (2012) · Structure · doi:10.1016/j.str.2012.04.009 · Cited by 139 · see citing works

The Cul3–KLHL21 E3 ubiquitin ligase targets Aurora B to midzone microtubules in anaphase and is required for cytokinesis

Maerki, S., Olma, M. H., Staubli, T., Steigemann, P., Gerlich, D. W., Quadroni, M., Sumara, I., & Peter, M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906117 · Cited by 133 · see citing works

Analysis of Drosophila Segmentation Network Identifies a JNK Pathway Factor Overexpressed in Kidney Cancer

Liu, J., Ghanim, M., Xue, L., Brown, C. D., Iossifov, I. H., Angeletti, C., Hua, S., Negre, N. N., Ludwig, M., Stricker, T. P., et al. (2009) · Science · doi:10.1126/science.1157669 · Cited by 125 · see citing works

Arabidopsisα Aurora Kinases Function in Formative Cell Division Plane Orientation

Damme, D. V., Rybel, B. D., Gudesblat, G. E., et al. (2011) · The Plant Cell · doi:10.1105/tpc.111.089565 · Cited by 121 · see citing works

The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses

Lee, Y.-R., Yuan, W.-C., Ho, H.-C., Chen, C.-H., Shih, H., & Chen, R. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.62 · Cited by 120 · see citing works

Large-Scale, Lineage-Specific Expansion of a Bric-a-Brac/Tramtrack/Broad Complex Ubiquitin-Ligase Gene Family in Rice

Gingerich, D. J., Hanada, K., Shiu, S., & Vierstra, R. D. (2007) · The Plant Cell · doi:10.1105/tpc.107.051300 · Cited by 120 · see citing works

Ubiquitylation-dependent localization of PLK1 in mitosis

Beck, J., Maerki, S., Posch, M., Metzger, T., Persaud, A. K., Scheel, H., Hofmann, K., Rotin, D., Pedrioli, P. G. A., Swedlow, J. R., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2695 · Cited by 119 · see citing works

Mutation of a potassium channel–related gene in progressive myoclonic epilepsy

Bogaert, P. V., Azizieh, R., Désir, J., Aeby, A., Meırleır, L. D., Laes, J., Christiaens, F. J. C., & Abramowicz, M. J. (2007) · Annals of Neurology · doi:10.1002/ana.21121 · Cited by 119 · see citing works

CAND1 controls in vivo dynamics of the cullin 1-RING ubiquitin ligase repertoire

Wu, S., Zhu, W., Nhan, T., Toth, J. I., Petroski, M. D., & Wolf, D. A. (2013) · Nature Communications · doi:10.1038/ncomms2636 · Cited by 118 · see citing works

A Homozygous Mutation in KCTD7 Links Neuronal Ceroid Lipofuscinosis to the Ubiquitin-Proteasome System

Staropoli, J. F., Karaa, A., Lim, E. T., Kirby, A. W., Elbalalesy, N., Romansky, S. G., Leydiker, K., Coppel, S., Barone, R., Xin, W. W., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.05.023 · Cited by 115 · see citing works

Emerging regulatory mechanisms in ubiquitin-dependent cell cycle control

Mocciaro, A., & Rapé, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.091199 · Cited by 110 · see citing works

Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants

Chen, L., Lee, J. H., Weber, H. H., Tohge, T., Witt, S., Roje, S., Fernie, A. R., & Hellmann, H. A. (2013) · The Plant Cell · doi:10.1105/tpc.112.107292 · Cited by 110 · see citing works

Arabidopsis CULLIN3 Genes Regulate Primary Root Growth and Patterning by Ethylene-Dependent and -Independent Mechanisms

Thomann, A., Lechner, E., Hansen, M., Dumbliauskas, E., Parmentier, Y., Kieber, J. J., Scheres, B., & Genschik, P. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000328 · Cited by 106 · see citing works

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 101 · see citing works

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 101 · see citing works

Microtubule-associated protein 1B

Ding, J., Liu, J., Kowal, A. S., et al. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200202055 · Cited by 101 · see citing works

Cullin-3 Regulates Vascular Smooth Muscle Function and Arterial Blood Pressure via PPARγ and RhoA/Rho-Kinase

Pelham, C. J., Ketsawatsomkron, P., Groh, S., Grobe, J. L., de Lange, W. J., Ibeawuchi, S., Keen, H. L., Weatherford, E. T., Faraci, F. M., & Sigmund, C. D. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.08.011 · Cited by 100 · see citing works

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 · see citing works

Molecular and functional characterization of Arabidopsis Cullin 3A

Dieterle, M., Thomann, A., Renou, J., Parmentier, Y., Cognat, V., Lemonnier, G., Müller, R., Shen, W., Kretsch, T., & Genschik, P. (2004) · The Plant Journal · doi:10.1111/j.1365-313x.2004.02302.x · Cited by 99 · see citing works

Large-scale detection of ubiquitination substrates using cell extracts and protein microarrays

Merbl, Y., & Kirschner, M. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812892106 · Cited by 97 · see citing works

Polar-localized NPH3-like proteins regulate polarity and endocytosis of PIN-FORMED auxin efflux carriers

Furutani, M., Sakamoto, N., Yoshida, S. M., Kajiwara, T., Robert, H. S., Friml, J., & Tasaka, M. (2011) · Development · doi:10.1242/dev.057745 · Cited by 93 · see citing works

Pcif1 modulates Pdx1 protein stability and pancreatic β cell function and survival in mice

Claiborn, K. C., Sachdeva, M. M., Cannon, C. E., Groff, D., Singer, J. D., & Stoffers, D. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40440 · Cited by 87 · see citing works

KEL-8 Is a Substrate Receptor for CUL3-dependent Ubiquitin Ligase That Regulates Synaptic Glutamate Receptor Turnover

Schaefer, H., & Rongo, C. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0794 · Cited by 83 · see citing works

Coordinated Activation of the Nuclear Ubiquitin Ligase Cul3-SPOP by the Generation of Phosphatidylinositol 5-Phosphate

Bunce, M. W., Boronenkov, I. V., & Anderson, R. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710222200 · Cited by 80 · see citing works

Kelch-like homologue 9 mutation is associated with an early onset autosomal dominant distal myopathy

Çırak, S., von Deimling, F., Sachdev, S., Errington, W. J., Herrmann, R., Bönnemann, C. G., Brockmann, K., Hinderlich, S., Lindner, T. H., Steinbrecher, A., et al. (2010) · Brain · doi:10.1093/brain/awq108 · Cited by 75 · see citing works

Selective proteolysis sets the tempo of the cell cycle

Marrocco, K., Bergdoll, M., Achard, P., Criqui, M., & Genschik, P. (2010) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2010.07.004 · Cited by 73 · see citing works

Progressive Myoclonic Epilepsy-Associated Gene KCTD7 is a Regulator of Potassium Conductance in Neurons

Azizieh, R., Orduz, D., Bogaert, P. V., Bouschet, T., Rodriguez, W., Schiffmann, S. N., Pirson, I., & Abramowicz, M. J. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8194-0 · Cited by 69 · see citing works

The Light-Response BTB1 and BTB2 Proteins Assemble Nuclear Ubiquitin Ligases That Modify Phytochrome B and D Signaling in Arabidopsis

Christians, M. J., Gingerich, D. J., Hua, Z., Lauer, T., & Vierstra, R. D. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.199109 · Cited by 69 · see citing works

Arabidopsis <i>CUL3A</i> and <i>CUL3B</i> genes are essential for normal embryogenesis

Thomann, A., Brukhin, V., Dieterle, M., Gheyeselinck, J., Vantard, M., Grossniklaus, U., & Genschik, P. (2005) · The Plant Journal · doi:10.1111/j.1365-313x.2005.02467.x · Cited by 65 · see citing works

The Cullin7 E3 ubiquitin ligase: A novel player in growth control

Sarikas, A., Xu, X., Field, L. J., & Pan, Z. (2008) · Cell Cycle · doi:10.4161/cc.7.20.6922 · Cited by 64 · see citing works

Germline-Specific MATH-BTB Substrate Adaptor MAB1 Regulates Spindle Length and Nuclei Identity in Maize

Juranić, M., Srilunchang, K.-O., Krohn, N. G., Leljak-Levanić, D., Sprunck, S., & Dresselhaus, T. (2012) · The Plant Cell · doi:10.1105/tpc.112.107169 · Cited by 64 · see citing works

Cullin-3 regulates late endosome maturation

Huotari, J., Meyer‐Schaller, N., Hubner, M., Stauffer, S., Katheder, N. S., Horváth, P., Mancini, R., Helenius, A., & Peter, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118744109 · Cited by 63 · see citing works

BAZF, a novel component of cullin3-based E3 ligase complex, mediates VEGFR and Notch cross-signaling in angiogenesis

Ohnuki, H., Inoue, H., Takemori, N., et al. (2012) · Blood · doi:10.1182/blood-2011-03-345306 · Cited by 63 · see citing works

Phototropism: Mechanism and Outcomes

Pedmale, U. V., Celaya, R. B., & Liscum, E. (2010) · The Arabidopsis Book · doi:10.1199/tab.0125 · Cited by 63 · see citing works

Genetic Disruption of KEAP1/CUL3 E3 Ubiquitin Ligase Complex Components is a Key Mechanism of NF-KappaB Pathway Activation in Lung Cancer

Thu, K. L., Pikor, L. A., Chari, R., Wilson, I. M., MacAulay, C. E., English, J. C., Tsao, M., Gazdar, A. F., Lam, S. C., Lam, W. L., et al. (2011) · Journal of Thoracic Oncology · doi:10.1097/jto.0b013e3182289479 · Cited by 60 · see citing works

Ubiquitin Ligase Activity of Cul3-KLHL7 Protein Is Attenuated by Autosomal Dominant Retinitis Pigmentosa Causative Mutation

Kigoshi, Y., Tsuruta, F., & Chiba, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.245126 · Cited by 60 · see citing works

A Role for Saccharomyces cerevisiae Cul8 Ubiquitin Ligase in Proper Anaphase Progression

Michel, J. J. C., McCarville, J. F., & Xiong, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210358200 · Cited by 56 · see citing works

Molecular organization of the cullin E3 ligase adaptor KCTD11

Correale, S., Pirone, L., Marcotullio, L. D., Smaele, E. D., Greco, A., Mazzà, D., Moretti, M., Alterio, V., Vitagliano, L., Gaetano, S. D., et al. (2011) · Biochimie · doi:10.1016/j.biochi.2010.12.014 · Cited by 54 · see citing works

A feedback loop mediated by degradation of an inhibitor is required to initiate neuronal differentiationPreprint

Sobieszczuk, D. F., Poliakov, A. A., Xu, Q., & Wilkinson, D. G. (2010) · Genes & Development · doi:10.1101/gad.554510 · Cited by 54 · see citing works

The Cul3/Klhdc5 E3 Ligase Regulates p60/Katanin and Is Required for Normal Mitosis in Mammalian Cells

Cummings, C. M., Bentley, C. A., Perdue, S. A., Baas, P. W., & Singer, J. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809374200 · Cited by 52 · see citing works

The cyclin E regulator cullin 3 prevents mouse hepatic progenitor cells from becoming tumor-initiating cells

Kossatz-Boehlert, U., Breuhahn, K., Wolf, B., Hardtke‐Wolenski, M., Wilkens, L., Steinemann, D., Singer, S., Brass, F., Kubicka, S., Schlegelberger, B., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41959 · Cited by 51 · see citing works

KBTBD13 interacts with Cullin 3 to form a functional ubiquitin ligase

Sambuughin, N., Świętnicki, W., Techtmann, S. M., Matrosova, V. Y., Wallace, T., Goldfarb, L. G., & Maynard, E. L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.074 · Cited by 41 · see citing works

Control of Rapsyn Stability by the CUL-3-containing E3 Ligase Complex

Nam, S., Min, K., Hwang, H., Lee, H., Lee, J. H., 윤종복, Lee, H., Park, S., & Lee, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808230200 · Cited by 33 · see citing works

Cullin 3 mediates SRC-3 ubiquitination and degradation to control the retinoic acid response

Ferry, C., Gaouar, S., Fischer, B., Boeglin, M., Paul, N., Samarut, E., Piskunov, A., Pankotai-Bodo, G., Brino, L., & Rochette-Egly, C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102572108 · Cited by 33 · see citing works

A Quantitative Proteomic Analysis Uncovers the Relevance of CUL3 in Bladder Cancer Aggressiveness

Grau, L., Luque-Garcia, J. L., González‐Peramato, P., Theodorescu, D., Palou, J., Gómez, J. M. F., & Sänchez‐Carbayo, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053328 · Cited by 25 · see citing works

Cullins and cell cycle control

Gieffers, C., Schleiffer, A., & Peters, J. M. (2000) · PROTOPLASMA · doi:10.1007/bf01279896 · Cited by 13 · see citing works

Cyclin D–CDK4 kinase destabilizes PD-L1 via cullin 3–SPOP to control cancer immune surveillance

Zhang, J., Bu, X., Wang, H., Zhu, Y., Geng, Y., Nihira, N. T., Tan, Y., Ci, Y., Wu, F., Dai, X., et al. (2018) · Nature · doi:10.1038/nature25015 · Cited by 1,013 · see citing works

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 · see citing works

Mechanisms of synaptic transmission dysregulation in the prefrontal cortex: pathophysiological implications

Yan, Z., & Rein, B. (2022) · Molecular Psychiatry · doi:10.1038/s41380-021-01092-3 · Cited by 300 · see citing works

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 · see citing works

16p11.2 Copy Number Variations and Neurodevelopmental Disorders

Rein, B., & Yan, Z. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.09.001 · Cited by 160 · see citing works

Spatiotemporal 16p11.2 protein network implicates cortical late mid-fetal brain development and KCTD13-Cul3-RhoA pathway in psychiatric diseases

Lin, G. N., Corominas, R., Lemmens, I., Yang, X., Tavernier, J., Hill, D. E., Vidal, M., Sebat, J., & Iakoucheva, L. M. (2015) · Neuron · doi:10.1016/j.neuron.2015.01.010 · Cited by 155 · see citing works

Harnessing the E3 Ligase KEAP1 for Targeted Protein Degradation

Wei, J., Meng, F., Park, K.-S., Yim, H., Velez, J., Kumar, P., Wang, L., Xie, L., Chen, H., Shen, Y., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c04841 · Cited by 154 · see citing works

Regulation of the CUL3 Ubiquitin Ligase by a Calcium-Dependent Co-adaptor

McGourty, C. A., Akopian, D., Walsh, C., Gorur, A., Werner, A., Schekman, R., Bautista, D., & Rape, M. (2016) · Cell · doi:10.1016/j.cell.2016.09.026 · Cited by 126 · see citing works

Behavioral, circuitry, and molecular aberrations by region-specific deficiency of the high-risk autism gene Cul3

Rapanelli, M., Tan, T., Wang, W., Wang, X., Wang, Z.-J., Zhong, P., Frick, L., Qin, L., Ma, K., Qu, J., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-019-0498-x · Cited by 74 · see citing works

Structural and biochemical characterization of the KLHL3–WNK kinase interaction important in blood pressure regulation

Schumacher, F.-R., Sorrell, F. J., Alessi, D. R., Bullock, A. N., & Kurz, T. (2014) · Biochemical Journal · doi:10.1042/bj20140153 · Cited by 76 · see citing works

KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated PML and DAPK ubiquitination

Chen, H. Y., Hu, J. Y., Chen, T. H., Lin, Y. C., Liu, X., Lin, M. Y., Lang, Y. D., Yen, Y., & Chen, R. H. (2015) · Oncogene · doi:10.1038/onc.2014.435 · Cited by 39 · see citing works

Structural Basis for Recruitment of DAPK1 to the KLHL20 E3 Ligase

Chen, Z., Picaud, S., Filippakopoulos, P., D'Angiolella, V., & Bullock, A. N. (2019) · Structure · doi:10.1016/j.str.2019.06.005 · Cited by 37 · see citing works

Cullin 3, a cellular scripter of the non-proteolytic ubiquitin code

Jerabkova, K., & Sumara, I. (2019) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2018.12.007 · Cited by 33 · see citing works

Arabidopsis ROOT PHOTOTROPISM2 Is a Light-Dependent Dynamic Modulator of Phototropin1

Kimura, T., Tsuchida-Mayama, T., Imai, H., Okajima, K., Ito, K., & Sakai, T. (2020) · The Plant Cell · doi:10.1105/tpc.19.00926 · Cited by 22 · see citing works

Functional Significance of the E3 Ubiquitin Ligases in Disease and Therapeutics

Dongdem, J. T., & Wezena, C. A. (2021) · Biochemistry · doi:10.5772/intechopen.100534 · Cited by 5 · see citing works

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C

Paluda, A., Middleton, A. J., Roßig, C., Mace, P. D., & Day, C. L. (2022) · Nature Communications · doi:10.1038/s41467-022-28782-y · Cited by 32 · see citing works

Functional analysis of the ubiquitin ligase Hrd1p with the ubiquitin -conjugating enzyme Ubc7p

Bazirgan, O. A. (2007) · eScholarship (California Digital Library)

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Liu, S., Chen, Y., Li, J., Huang, T., Tarasov, S. G., King, A., Weissman, A. M., Byrd, R. A., & Das, R. (2012) · Structure · doi:10.1016/j.str.2012.09.020 · Cited by 31 · see citing works

Analysis of ubiquitin E3 ligase activity using selective polyubiquitin binding proteins

Marblestone, J. G., LaRocque, J. P., Mattern, M. R., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.06.013 · Cited by 18 · see citing works