Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
Open accessAbstract
Hundreds of human cullin-RING E3 ligases (CRLs) modify thousands of proteins with ubiquitin (UB) to achieve vast regulation. Current dogma posits that CRLs first catalyze UB transfer from an E2 to their client substrates and subsequent polyubiquitylation from various linkage-specific E2s. We report an alternative E3-E3 tagging cascade: many cellular NEDD8-modified CRLs associate with a mechanistically distinct thioester-forming RBR-type E3, ARIH1, and rely on ARIH1 to directly add the first UB and, in some cases, multiple additional individual monoubiquitin modifications onto CRL client substrates. Our data define ARIH1 as a component of the human CRL system, demonstrate that ARIH1 can efficiently and specifically mediate monoubiquitylation of several CRL substrates, and establish principles for how two distinctive E3s can reciprocally control each other for simultaneous and joint regulation of substrate ubiquitylation. These studies have broad implications for CRL-dependent proteostasis and mechanisms of E3-mediated UB ligation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
RING and RBR ligases have recently been shown to work in unison to mediate substrate ubiquitylation in a site-specific manner.
“RING and RBR ligases have recently been shown to work in unison to mediate substrate ubiquitylation in a site-specific manner116,117.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [116]
KLHL12 can assemble with specific co-adaptors to monoubiquitylate SEC31 for collagen trafficking.
“it can also assemble with specific co-adaptors to monoubiquitylate the COPII component SEC31 for collagen trafficking 90,91,92”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [91]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
Soucy, T. A., Smith, P. G., Milhollen, M. A., Berger, A. J., Gavin, J. M., Adhikari, S., Brownell, J. E., Burke, K. E., Cardin, D. P., Critchley, S., et al. (2009) · Nature · doi:10.1038/nature07884 · Cited by 1,990 · see citing works
Identification and characterization of essential genes in the human genome
Wang, T., Birsoy, K., Hughes, N. W., Krupczak, K. M., Post, Y., Wei, J. J., Lander, E. S., & Sabatini, D. M. (2015) · Science · doi:10.1126/science.aac7041 · Cited by 1,617 · see citing works
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,582 · see citing works
Self-citationHigh-Resolution CRISPR Screens Reveal Fitness Genes and Genotype-Specific Cancer Liabilities.
Hart, T., Chandrashekhar, M., Aregger, M., Steinhart, Z., Brown, K. R., MacLeod, G., Mis, M., Zimmermann, M., Fradet-Turcotte, A., Sun, S., et al. (2015) · Cell · doi:10.1016/j.cell.2015.11.015 · Cited by 1,571 · see citing works
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 1,512 · see citing works
Self-citationStructure 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 · see citing works
Self-citationThe BioPlex network: a systematic exploration of the human interactome
Huttlin, E. L., Ting, L., Bruckner, R. J., Gebreab, F., Gygi, M. P., Szpyt, J., Tam, S., Zarraga, G., Colby, G., Baltier, K., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.043 · Cited by 1,425 · cited 34× · see citing works
“As with WT ARIH1, ARIH1OPEN-OFF associated with many CRL SRs and SEC13-SEC31A yet exhibited a smaller fold change in interactions compared to WT and C357S ARIH1 following 2-hr treatment with MLN4924 (Figures S7B and S7C).”
InfluentialSelf-citationMcAlister, G. C., Nusinow, D. P., Jedrychowski, M. P., Wühr, M., Huttlin, E. L., Erickson, B. K., Rad, R., Haas, W., & Gygi, S. P. (2014) · Analytical Chemistry · doi:10.1021/ac502040v · Cited by 1,263 · see citing works
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,056 · see citing works
A ubiquitin ligase complex assembles linear polyubiquitin chains
Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., & Iwaï, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601360 · Cited by 772 · see citing works
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
Self-citationNew insights into ubiquitin E3 ligase mechanism
Berndsen, C., & Wolberger, C. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2780 · Cited by 706 · see citing works
Phosphorylation‐dependent degradation of the cyclin‐dependent kinase inhibitor p27Kip1
Vlach, J., Hennecke, S., & Amati, B. B. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5334 · Cited by 680 · see citing works
RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.026 · Cited by 608 · see citing works
UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
Wenzel, D. M., Lissounov, A., Brzović, P. S., & Klevit, R. E. (2011) · Nature · doi:10.1038/nature09966 · Cited by 560 · see citing works
Busino, L., Bassermann, F. C., Maiolica, A., Lee, C., Nolan, P. M., Godinho, S. I. H., Draetta, G. F., & Pagano, M. (2007) · Science · doi:10.1126/science.1141194 · Cited by 509 · see citing works
Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W., & Pavletich, N. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.022 · Cited by 464 · see citing works
Self-citationFunctional Genomic Landscape of Human Breast Cancer Drivers, Vulnerabilities, and Resistance
Marcotte, R., Sayad, A., Brown, K. R., Sanchez-Garcia, F., Reimand, J., Haider, M., Virtanen, C., Bradner, J. E., Bader, G. D., Mills, G. B., et al. (2016) · Cell · doi:10.1016/j.cell.2015.11.062 · Cited by 439 · see citing works
Global Identification of Modular Cullin-RING Ligase Substrates
Emanuele, M. J., Elia, A. E. H., Xu, Q., Thoma, C. R., Izhar, L., Leng, Y., Guo, A., Chen, Y., Rush, A. J., Hsu, P. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.019 · Cited by 403 · 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
Self-citationYoo, S. H., Mohawk, J. A., Siepka, S. M., Shan, Y., Huh, S. K., Hong, H., Kornblum, I., Kumar, V., Koike, N., Xu, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.055 · Cited by 341 · 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
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
Self-citationCand1 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
Sequential E2s Drive Polyubiquitin Chain Assembly on APC Targets
Rodrigo-Brenni, M. C., & Morgan, D. O. (2007) · Cell · doi:10.1016/j.cell.2007.05.027 · Cited by 250 · see citing works
SCFFBXL3 ubiquitin ligase targets cryptochromes at their cofactor pocket
Xing, W., Busino, L., Hinds, T. R., Marionni, S. T., Saifee, N. H., Bush, M. F., Pagano, M., & Zheng, N. (2013) · Nature · doi:10.1038/nature11964 · Cited by 234 · see citing works
An Allosteric Inhibitor of the Human Cdc34 Ubiquitin-Conjugating Enzyme
Ceccarelli, D. F. J., Tang, X., Pelletier, B., Orlicky, S. M., Xie, W., Plantevin, V., Neculai, D., Chou, Y.-C., Ogunjimi, A. A., Al-Hakim, A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.05.039 · Cited by 234 · see citing works
Structural assembly of cullin-RING ubiquitin ligase complexes
Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227 · see citing works
Self-citationDown-regulation of p27 by Two Mechanisms, Ubiquitin-mediated Degradation and Proteolytic Processing
Shirane, M., Harumiya, Y., Ishida, N., Hirai, A., Miyamoto, C., Hatakeyama, S., Nakayama, K. I., & Kitagawa, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13886 · Cited by 226 · 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
Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation
Lechtenberg, B. C., Rajput, A., Sanishvili, R., Dobaczewska, M. K., Ware, C. F., Mace, P. D., & Riedl, S. J. (2016) · Nature · doi:10.1038/nature16511 · Cited by 208 · see citing works
Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
Stieglitz, B., Rana, R. R., Koliopoulos, M. G., Morris-Davies, A. C., Schaeffer, V., Christodoulou, E., Howell, S. A., Brown, N. R., Đikić, I., & Rittinger, K. (2013) · Nature · doi:10.1038/nature12638 · Cited by 202 · see citing works
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 · see citing works
Self-citationKleiger, G., Saha, A., Lewis, S. M., Kuhlman, B. A., & Deshaies, R. J. (2009) · Cell · doi:10.1016/j.cell.2009.10.030 · Cited by 194 · see citing works
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 165 · see citing works
Hwang, C., Shemorry, A., Auerbach, D., & Varshavsky, A. J. (2010) · Nature Cell Biology · doi:10.1038/ncb2121 · Cited by 147 · see citing works
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I. V., Miller, D. J., Nourse, A., Alpi, A. F., & Schulman, B. A. (2013) · Structure · doi:10.1016/j.str.2013.04.019 · Cited by 140 · see citing works
Self-citationPriming and Extending: A UbcH5/Cdc34 E2 Handoff Mechanism for Polyubiquitination on a SCF Substrate
Wu, K., Kovacev, J., & Pan, Z.-Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.025 · Cited by 126 · 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
Moynihan, T. P., Ardley, H. C., Nuber, U. A., Rose, S. A., Jones, P. F., Markham, A. F., Scheffner, M., & Robinson, P. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30963 · Cited by 117 · see citing works
A comprehensive method for detecting ubiquitinated substrates using TR-TUBE
Yoshida, Y., Saeki, Y., Murakami, A., Kawawaki, J., Tsuchiya, H., Yoshihara, H., Shindo, M., & Tanaka, K. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422313112 · Cited by 117 · see citing works
TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin‐RING ligase complexes
Kelsall, I. R., Duda, D. M., Olszewski, J. L., Hofmann, K., Knebel, A., Langevin, F., Wood, N. T., Wightman, M., Schulman, B. A., & Alpi, A. F. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.209 · Cited by 111 · see citing works
Self-citationCSN- 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
Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms
Dove, K. K., Stieglitz, B., Duncan, E. D., Rittinger, K., & Klevit, R. E. (2016) · EMBO Reports · doi:10.15252/embr.201642641 · Cited by 100 · see citing works
Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail
Yamoah, K., Oashi, T., Sarikas, A., Gazdoiu, S., Osman, R., & Pan, Z. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806155105 · Cited by 98 · see citing works
Regulating the Regulators: Recent Revelations in the Control of E3 Ubiquitin Ligases
Vittal, V., Stewart, M. D., Brzović, P. S., & Klevit, R. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.675165 · Cited by 88 · see citing works
Pathogenic Bacteria Target NEDD8-Conjugated Cullins to Hijack Host-Cell Signaling Pathways
Jubelin, G., Taieb, F. E., Duda, D. M., Hsu, Y., Samba‐Louaka, A., Nobe, R., Pénary, M., Watrin, C., Nougayrède, J., Schulman, B. A., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001128 · Cited by 81 · see citing works
Self-citationUnderstanding Cullin-RING E3 Biology through Proteomics-based Substrate Identification
Harper, J. W., & Tan, M.-K. M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r112.021154 · Cited by 71 · see citing works
Self-citationLee, J. E., Sweredoski, M. J., Graham, R. L. J., Kolawa, N. J., Smith, G. T., Hess, S. Y., & Deshaies, R. J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.006460 · Cited by 60 · see citing works
Yu, C., Mao, H., Novitsky, E. J., Tang, X., Rychnovsky, S. D., Zheng, N., & Huang, L. (2015) · Nature Communications · doi:10.1038/ncomms10053 · Cited by 43 · see citing works
RBR Ubiquitin Ligases: Diversification and Streamlining in Animal Lineages
Marı́n, I. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9252-3 · Cited by 36 · see citing works
Implicating SCF Complexes in Organogenesis in Caenorhabditis elegans
Polley, S. R. G., Kuzmanov, A., Kuang, J., Karpel, J. E., Lažetić, V., Karina, E. I., Veo, B. L., & Fay, D. S. (2013) · Genetics · doi:10.1534/genetics.113.158485 · Cited by 10 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works
Targeted protein degradation: expanding the toolbox
Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works
The logic of the 26S proteasome.
Collins, G. A., & Goldberg, A. L. (2017) · Cell · doi:10.1016/j.cell.2017.04.023 · Cited by 933 · see citing works
Bouchard, J. J., Otero, J. H., Scott, D. C., Szulc, E., Martin, E. W., Sabri, N., Granata, D., Marzahn, M. R., Lindorff‐Larsen, K., Salvatella, X., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.027 · Cited by 382 · see citing works
Self-citationParkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells
Villa, E., Proïcs, E., Rubio‐Patiño, C., Obba, S., Zunino, B., Bossowski, J. P., Rozier, R., Chiche, J., Mondragón, L., Riley, J. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.087 · Cited by 315 · see citing works
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 · see citing works
Self-citationCullin-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 252 · see citing works
Self-citationA ubiquitin ligase mediates target-directed microRNA decay independently of tailing and trimming
Han, J., LaVigne, C. A., Jones, B. T., Zhang, H., Gillett, F. A., & Mendell, J. T. (2020) · Science · doi:10.1126/science.abc9546 · Cited by 235 · see citing works
No Parkin Zone: Mitophagy without Parkin
Villa, E., Marchetti, S., & Ricci, J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.004 · Cited by 221 · see citing works
Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
Horn-Ghetko, D., Krist, D. T., Prabu, J. R., Baek, K., Mulder, M. P. C., Klügel, M., Scott, D. C., Ovaa, H., Kleiger, G., & Schulman, B. A. (2021) · Nature · doi:10.1038/s41586-021-03197-9 · Cited by 187 · see citing works
Self-citationKelsall, I. R., Zhang, J., Knebel, A., Arthur, J. S. C., & Cohen, P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905873116 · Cited by 152 · see citing works
Self-citationNEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Baek, K., Scott, D. C., & Schulman, B. A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.007 · Cited by 152 · see citing works
Self-citationBranching Out: Improved Signaling by Heterotypic Ubiquitin Chains
Haakonsen, D. L., & Rapé, M. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.06.003 · Cited by 147 · see citing works
RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns
Walden, H., & Rittinger, K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0063-3 · Cited by 139 · see citing works
RING-Between-RING E3 Ligases: Emerging Themes amid the Variations
Dove, K. K., & Klevit, R. E. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.08.008 · Cited by 140 · see citing works
<i>KCTD</i>: A new gene family involved in neurodevelopmental and neuropsychiatric disorders
Teng, X., Aouacheria, A., Lionnard, L., Metz, K. A., Soane, L., Kamiya, A., & Hardwick, J. M. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13156 · Cited by 124 · see citing works
Lampert, F., Stafa, D., Goga, A., Soste, M., Gilberto, S., Olieric, N., Picotti, P., Stoffel, M., & Peter, M. (2018) · eLife · doi:10.7554/elife.35528 · Cited by 123 · see citing works
ARIH1 signaling promotes anti-tumor immunity by targeting PD-L1 for proteasomal degradation
Wu, Y., Zhang, C., Liu, X., He, Z., Shan, B., Zeng, Q., Zhao, Q., Zhu, H., Liao, H., Cen, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22467-8 · Cited by 117 · see citing works
Blocking an N-terminal acetylation–dependent protein interaction inhibits an E3 ligase
Scott, D. C., Hammill, J. T., Min, J., Rhee, D. Y., Connelly, M., Sviderskiy, V. O., Bhasin, D., Chen, Y., Ong, S. S., Chai, S. C., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2386 · Cited by 108 · see citing works
Self-citationKumar, A., Chaugule, V. K., Condos, T., Barber, K. R., Johnson, C., Toth, R. L., Sundaramoorthy, R., Knebel, A., Shaw, G. S., & Walden, H. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3400 · Cited by 109 · see citing works
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 · see citing works
Enzymatic Logic of Ubiquitin Chain Assembly
Deol, K. K., Lorenz, S., & Strieter, E. R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00835 · Cited by 107 · see citing works
RBR E3 ubiquitin ligases in tumorigenesis
Wang, P., Dai, X., Jiang, W., Li, Y., & Wei, W. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.05.002 · Cited by 105 · see citing works
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 92 · see citing works
The HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC
Fuseya, Y., Fujita, H., Kim, M., Ohtake, F., Nishide, A., Sasaki, K., Saeki, Y., Tanaka, K., Takahashi, R., & Iwaï, K. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0517-9 · Cited by 84 · see citing works
Insights in Post-Translational Modifications: Ubiquitin and SUMO
Salas‐Lloret, D., & González‐Prieto, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063281 · Cited by 88 · see citing works
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 87 · see citing works
Dynamic ubiquitin signaling in cell cycle regulation
Gilberto, S., & Peter, M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201703170 · Cited by 86 · see citing works
Goeman, F., Nicola, F. D., Scalera, S., Sperati, F., Gallo, E., Ciuffreda, L., Pallocca, M., Pizzuti, L., Krasniqi, E., Barchiesi, G., et al. (2019) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2019.07.003 · Cited by 86 · see citing works
MARCH6 and TRC8 facilitate the quality control of cytosolic and tail‐anchored proteins
Stefanovic-Barrett, S., Dickson, A. S., Burr, S. P., Williamson, J. C., Lobb, I. T., van den Boomen, D. J. H., Lehner, P. J., & Nathan, J. A. (2018) · EMBO Reports · doi:10.15252/embr.201745603 · Cited by 80 · see citing works
A new dawn beyond lysine ubiquitination
Squair, D. R., & Virdee, S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01088-2 · Cited by 81 · see citing works
Robust cullin-RING ligase function is established by a multiplicity of poly-ubiquitylation pathways
Hill, S., Reichermeier, K. M., Scott, D. C., Samentar, L., Coulombe‐Huntington, J., Izzi, L., Tang, X., Ibarra, R., Bertomeu, T., Moradian, A., et al. (2019) · eLife · doi:10.7554/elife.51163 · Cited by 80 · see citing works
Self-citationUBE2G1 governs the destruction of cereblon neomorphic substrates
Lu, G., Weng, S., Matyskiela, M., Zheng, X., Fang, W., Wood, S., Surka, C., Mizukoshi, R., Lu, C.-C., Mendy, D., et al. (2018) · eLife · doi:10.7554/elife.40958 · Cited by 78 · see citing works
Julian, J., Coego, A., Lozano‐Juste, J., Lechner, E., Wu, Q., Zhang, X., Merilo, E., Belda‐Palazón, B., Park, S., Cutler, S. R., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908677116 · Cited by 79 · see citing works
Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation
Dubiel, W., Dubiel, D., Wolf, D. A., & Naumann, M. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.010 · Cited by 73 · see citing works
Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5
Hehl, L. A., Horn‐Ghetko, D., Prabu, J. R., Vollrath, R., Vu, D. T., Berrocal, D. A. P., Mulder, M. P. C., van Noort, G. J. V. D. H., & Schulman, B. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01414-2 · Cited by 72 · see citing works
Self-citationThe CRL5–SPSB3 ubiquitin ligase targets nuclear cGAS for degradation
Xu, P., Liu, Y., Liu, C., Guey, B., Li, L., Mélénec, P., Ricci, J., & Ablasser, A. (2024) · Nature · doi:10.1038/s41586-024-07112-w · Cited by 77 · see citing works
Xiong, T.-C., Wei, M., Li, F., Shi, M., Gan, H., Tang, Z., Dong, H., Liuyu, T., Gao, P., Zhong, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33671-5 · Cited by 70 · see citing works
Chain reactions: molecular mechanisms of RBR ubiquitin ligases
Cotton, T. R., & Lechtenberg, B. C. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200237 · Cited by 67 · see citing works
Recruitment of FBXO22 for targeted degradation of NSD2
Nie, Y., Tabor, J. R., Li, J., Kutera, M., St‐Germain, J. R., Hanley, R. P., Wolf, E., Paulаkonis, E., Kenney, T. M. G., Duan, S., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01660-y · Cited by 70 · see citing works
Targeting neddylation E2s: a novel therapeutic strategy in cancer
Zheng, Y., Guo, Y.-J., Wang, B., Wang, C., Mamun, M., Gao, Y., & Liu, H. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01070-w · Cited by 69 · see citing works
Wu, Q., Zhang, H., Yang, D., Min, Q., Wang, Y., Zhang, W., & Zhan, Q. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.71234 · Cited by 68 · see citing works
Expanding the host cell ubiquitylation machinery targeting cytosolic Salmonella
Polajnar, M., Dietz, M. S., Heilemann, M., & Behrends, C. (2017) · EMBO Reports · doi:10.15252/embr.201643851 · Cited by 68 · see citing works
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
Wang, X. S., Cotton, T. R., Trevelyan, S. J., Richardson, L. W., Lee, W. T., Silke, J., & Lechtenberg, B. C. (2023) · Nature Communications · doi:10.1038/s41467-023-35871-z · Cited by 64 · see citing works
CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation
Kostrhon, S., Prabu, J. R., Baek, K., Horn‐Ghetko, D., von Gronau, S., Klügel, M., Basquin, J., Alpi, A. F., & Schulman, B. A. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00858-8 · Cited by 62 · see citing works
Self-citationARIH2 Is a Vif-Dependent Regulator of CUL5-Mediated APOBEC3G Degradation in HIV Infection
Hüttenhain, R., Xu, J., Burton, L. A., Gordon, D. E., Hultquist, J. F., Johnson, J. R., Satkamp, L., Hiatt, J. B., Rhee, D. Y., Baek, K., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.05.008 · Cited by 64 · see citing works
Self-citationStructural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI
Yuan, L., Lv, Z., Atkison, J. H., & Olsen, S. K. (2017) · Nature Communications · doi:10.1038/s41467-017-00272-6 · Cited by 61 · see citing works
Guiding Mitotic Progression by Crosstalk between Post-translational Modifications
Cuijpers, S. A. G., & Vertegaal, A. C. O. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.02.004 · Cited by 58 · see citing works
Metz, K. A., Teng, X., Coppens, I., Lamb, H. M., Wagner, B. E., Rosenfeld, J. A., Chen, X., Zhang, Y., Kim, H. J., Meadow, M. E., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25351 · Cited by 62 · see citing works
Structural Biology of CRL Ubiquitin Ligases
Rusnac, D.-V., & Zheng, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_2 · Cited by 52 · see citing works
Kong, K.-Y. E., Fischer, B. M., Meurer, M., Kats, I., Li, Z., Rühle, F., Barry, J. D., Kirrmaier, D., Chevyreva, V., Luis, B.-J. S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.018 · Cited by 53 · see citing works
CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis
Samelson, A. J., Ariqat, N., McKetney, J., Rohanitazangi, G., Bravo, C., Bose, R., Travaglini, K. J., Lam, V. L., Goodness, D., Ta, T., et al. (2026) · Cell · doi:10.1016/j.cell.2025.12.038 · Cited by 65 · see citing works
O’Connor, H. F., & Huibregtse, J. M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2529-6 · Cited by 42 · see citing works
Glucose-induced CRL4COP1-p53 axis amplifies glycometabolism to drive tumorigenesis
Su, Y., Luo, Y., Zhang, P., Lin, H., Pu, W., Zhang, H., Wang, H., Hao, Y., Xiao, Y., Zhang, X., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.010 · Cited by 57 · see citing works
Ari-1 Regulates Myonuclear Organization Together with Parkin and Is Associated with Aortic Aneurysms
Tan, K. L., Haelterman, N. A. T., Kwartler, C. S., Regalado, E. S., Lee, P.-T., Nagarkar-Jaiswal, S., Guo, D., Duraine, L., Wangler, M. F., Bamshad, M. J., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.03.020 · Cited by 55 · see citing works
The ubiquitin ligation machinery in the defense against bacterial pathogens
Tripathi‐Giesgen, I., Behrends, C., & Alpi, A. F. (2021) · EMBO Reports · doi:10.15252/embr.202152864 · Cited by 51 · see citing works
Self-citationFernandez, M. A., Belda‐Palazón, B., Julian, J., Coego, A., Lozano‐Juste, J., Iñigo, S., Rodríguez, L., Bueso, E., Goossens, A., & Rodrı́guez, P. L. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.19.00898 · Cited by 56 · see citing works
A central role for regulated protein stability in the control of TFE3 and MITF by nutrients
Nardone, C., Palanski, B. A., Scott, D. C., Timms, R. T., Barber, K. W., Gu, X., Mao, A., Leng, Y., Watson, E. V., Schulman, B. A., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.013 · Cited by 50 · see citing works
Self-citationStructural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1
Dove, K. K., Olszewski, J. L., Martino, L., Duda, D. M., Wu, X. S., Miller, D. J., Reiter, K. H., Rittinger, K., Schulman, B. A., & Klevit, R. E. (2017) · Structure · doi:10.1016/j.str.2017.04.013 · Cited by 52 · see citing works
Self-citationK6-linked ubiquitylation marks formaldehyde-induced RNA-protein crosslinks for resolution
Rahmanto, A. S., Blum, C., Scalera, C., Heidelberger, J. B., Mesitov, M. V., Horn‐Ghetko, D., Gräf, J. F., Mikičić, I., Hobrecht, R., Orekhova, A., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.011 · Cited by 52 · see citing works
Self-citationPerception of viral infections and initiation of antiviral defence in rice
Huang, Y., Yang, J., Sun, X., Li, J., Cao, X., Yao, S., Han, Y., Chen, C., Du, L., Li, S., et al. (2025) · Nature · doi:10.1038/s41586-025-08706-8 · Cited by 52 · see citing works
Systemwide disassembly and assembly of SCF ubiquitin ligase complexes
Baek, K., Scott, D. C., Henneberg, L. T., King, M. T., Mann, M., & Schulman, B. A. (2023) · Cell · doi:10.1016/j.cell.2023.02.035 · Cited by 47 · see citing works
Self-citationAki, D., Li, H., Zhang, W., Zheng, M., Elly, C., Lee, J. H., Zou, W., & Liu, Y. (2018) · Nature Immunology · doi:10.1038/s41590-018-0137-8 · Cited by 48 · see citing works
Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting
Li, J., Purser, N., Liwocha, J., Scott, D. C., Byers, H. A., Steigenberger, B. A., Hill, S., Tripathi‐Giesgen, I., Hinkle, T. B., Hansen, F. M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.022 · Cited by 45 · see citing works
Self-citationMechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases
Liwocha, J., Li, J., Purser, N., Rattanasopa, C., Maiwald, S. A., Krist, D. T., Scott, D. C., Steigenberger, B. A., Prabu, J. R., Schulman, B. A., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01206-1 · Cited by 44 · see citing works
Self-citationHigher-order SPOP assembly reveals a basis for cancer mutant dysregulation
Cuneo, M. J., O’Flynn, B. G., Lo, Y., Sabri, N., & Mittag, T. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.033 · Cited by 43 · see citing works
Alkylamine-tethered molecules recruit FBXO22 for targeted protein degradation
Kagiou, C., Cisneros, J. A., Farnung, J., Liwocha, J., Offensperger, F., Dong, K. D., Yang, K., Tin, G., Horstmann, C. S., Hinterndorfer, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49739-3 · Cited by 43 · see citing works
Self-citationSugar-mediated non-canonical ubiquitination impairs Nrf1/NFE2L1 activation
Yoshida, Y., Takahashi, T., Ishii, N., Matsuo, I., Takahashi, S., Inoue, H., Endo, A., Tsuchiya, H., Okada, M., Ando, C., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.07.013 · Cited by 42 · see citing works
Who with whom: functional coordination of E2 enzymes by RING E3 ligases during poly‐ubiquitylation
Lips, C., Ritterhoff, T., Weber, A. J., Janowska, M. K., Mustroph, M., Sommer, T., & Klevit, R. E. (2020) · The EMBO Journal · doi:10.15252/embj.2020104863 · Cited by 43 · see citing works
Liu, P., Cong, X., Liao, S., Jia, X., Wang, X., Dai, W., Zhai, L., Zhao, L., Ji, J., Ni, D., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00827-7 · Cited by 43 · see citing works
Basis for metabolite-dependent Cullin-RING ligase deneddylation by the COP9 signalosome
Lin, H., Zhang, X., Liu, L., Fu, Q., Zang, C., Ding, Y., Su, Y., Xu, Z., He, S., Yang, X., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911998117 · Cited by 41 · see citing works
Ubiquitin chain-elongating enzyme UBE2S activates the RING E3 ligase APC/C for substrate priming
Martinez‐Chacin, R. C., Bodrug, T., Bolhuis, D. L., Kedziora, K. M., Bonacci, T., Ordureau, A., Gibbs, M. E., Weissmann, F., Qiao, R., Grant, G. D., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0424-6 · Cited by 41 · see citing works
Self-citationHughes, D. C., Goodman, C. A., Baehr, L. M., Gregorevic, P., & Bodine, S. C. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00457.2023 · Cited by 42 · see citing works
Howley, B. V., Mohanty, B. K., Dalton, A. C., Grelet, S., Karam, J. A. Q., Dincman, T. A., & Howe, P. H. (2022) · Oncogene · doi:10.1038/s41388-022-02199-9 · Cited by 37 · see citing works
Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase
Ito, F., Alvarez-Cabrera, A. L., Liu, S., Yang, H., Shiriaeva, A., Zhou, Z. H., & Chen, X. S. (2023) · Science Advances · doi:10.1126/sciadv.ade3168 · Cited by 37 · see citing works
Dove, K. K., Kemp, H. A., Bona, K. R. D., Reiter, K. H., Milburn, L. J., Camacho, D., Fay, D. S., Miller, D. L., & Klevit, R. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705060114 · Cited by 37 · see citing works
Sorting and Export of Proteins at the Endoplasmic ReticulumPreprint
Raote, I., Saxena, S., & Malhotra, V. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041258 · Cited by 37 · see citing works
Xu, S., Zhu, S., Wang, Y., Huang, J., Chen, M., Wu, Q., He, Y., Chen, D., & Yan, G. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0525-x · Cited by 36 · see citing works
Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
Liwocha, J., Krist, D. T., van Noort, G. J. V. D. H., Hansen, F. M., Truong, V. H., Karayel, Ö., Purser, N., Houston, D., Burton, N., Bostock, M. J., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-00696-0 · Cited by 35 · see citing works
Self-citationThe GSK-3β-FBXL21 Axis Contributes to Circadian TCAP Degradation and Skeletal Muscle Function
Wirianto, M., Yang, J., Kim, E., Gao, S., Paudel, K. R., Choi, J. M., Choe, J., Gloston, G. F., Ademoji, P., Parakramaweera, R., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108140 · Cited by 35 · see citing works
Coego, A., Julian, J., Lozano‐Juste, J., Pizzio, G. A., Alrefaei, A. F., & Rodrı́guez, P. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137103 · Cited by 32 · see citing works
Export Control: Post-transcriptional Regulation of the COPII Trafficking Pathway
Bisnett, B. J., Condon, B. M., Lamb, C. H., Georgiou, G. R., & Boyce, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.618652 · Cited by 30 · see citing works
Cell cycle regulation by complex nanomachines
Koliopoulos, M. G., & Alfieri, C. (2021) · FEBS Journal · doi:10.1111/febs.16082 · Cited by 31 · see citing works
High-throughput ligand diversification to discover chemical inducers of proximity
Shaum, J. B., Ordoño, M. M. I., Steen, E. A., Wenge, D. V., Cheong, H., Janowski, J., Hunkeler, M., Bilotta, E. M., Rutter, Z. J., Barta, P. A., et al. (2026) · Nature Chemical Biology · doi:10.1038/s41589-025-02137-2 · Cited by 30 · see citing works
Watson, E. R., Grace, C. R., Zhang, W., Miller, D. J., Davidson, I. F., Prabu, J. R., Yu, S., Bolhuis, D. L., Kulko, E. T., Vollrath, R., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902889116 · Cited by 30 · see citing works
Self-citationSt‐Cyr, D. J., Ceccarelli, D. F. J., Orlicky, S. M., van der Sloot, A. M., Tang, X., Kelso, S., Moore, S., James, C. A., Posternak, G., Coulombe‐Huntington, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abi5797 · Cited by 29 · see citing works
UBA6 and NDFIP1 regulate the degradation of ferroportin
Traeger, L., Wiegand, S. B., Sauer, A. J., Corman, B. H. P., Peneyra, K. M., Wunderer, F., Fischbach, A., Bagchi, A., Malhotra, R. K., Zapol, W. M., et al. (2021) · Haematologica · doi:10.3324/haematol.2021.278530 · Cited by 28 · see citing works
Xia, Y., Fujisawa, R., Deegan, T. D., Sonneville, R., & Labib, K. P. M. (2021) · The EMBO Journal · doi:10.15252/embj.2021108053 · Cited by 28 · see citing works
Hopf, L. V. M., Baek, K., Klügel, M., von Gronau, S., Xiong, Y., & Schulman, B. A. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00815-6 · Cited by 28 · see citing works
Self-citationActivity-based profiling of cullin–RING E3 networks by conformation-specific probes
Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., & Schulman, B. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01392-5 · Cited by 31 · see citing works
Self-citationBotsch, J. J., Junker, R., Sorgenfrei, M., Ogger, P. P., Stier, L. J., von Gronau, S., Murray, P. J., Seeger, M. A., Schulman, B. A., & Bräuning, B. (2024) · Nature Communications · doi:10.1038/s41467-023-44670-5 · Cited by 24 · see citing works
Self-citationLi, Z., Du, X., Wen, L., Yu, L., Qin, J., Chen, Z., Huang, Y., Wu, X., Luo, H., Lin, Y., et al. (2021) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2021.100948 · Cited by 26 · see citing works
Roles of Cullin-RING Ubiquitin Ligases in Cardiovascular Diseases
Diaz, S., Wang, K., Sjögren, B., & Liu, X. (2022) · Biomolecules · doi:10.3390/biom12030416 · Cited by 26 · see citing works
MicroRNA-154-5p regulates the HPV16 E7-pRb pathway in Cervical Carcinogenesis by targeting CUL2
Zhao, W., Liu, Y., Zhang, L., Ding, L., Li, Y., Zhang, H., Wang, T., & Hao, M. (2020) · Journal of Cancer · doi:10.7150/jca.45871 · Cited by 25 · see citing works
Ahel, J., Fletcher, A. J., Grabarczyk, D. B., Roitinger, E., Deszcz, L., Lehner, A., Virdee, S., & Clausen, T. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.10.443411 · Cited by 26 · see citing works
Li, F., Sun, H., Li, Y., Bai, X., Dong, X., Zhao, N., Meng, J., Sun, B., & Zhang, D. (2021) · BMC Cancer · doi:10.1186/s12885-021-09010-0 · Cited by 25 · see citing works
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 23 · see citing works
Keap1-Nrf2 Heterodimer: A Therapeutic Target to Ameliorate Sickle Cell Disease
Chauhan, W., & Zennadi, R. (2023) · Antioxidants · doi:10.3390/antiox12030740 · Cited by 27 · see citing works
Li, J., Li, H., Zhao, J.-J., Yang, P. F., Xiang, X., Wei, S.-Y., Wang, T., Shi, Y.-J., Huang, J., & He, F. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128108 · Cited by 25 · see citing works
Probing ubiquitin and SUMO conjugation and deconjugation
Ovaa, H., & Vertegaal, A. C. O. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170086 · Cited by 23 · see citing works
Self-citation
- Authors
- Scott, D. C., Rhee, D. Y., Duda, D. M., Kelsall, I. R., Olszewski, J. L., Paulo, J. A., de Jong, A., Ovaa, H., Alpi, A. F., Harper, J. W., & Schulman, B. A.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Harvard University (US)
- MRC Protein Phosphorylation and Ubiquitylation Unit (GB)
- Leiden University Medical Center (NL)
- Corresponding author
- Harper, J. Wade
- Schulman, Brenda A.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2016-08
- Volume
- 166
- Issue
- 5
- Pages
- 1198-1214.e24
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5091668
- OpenAlex
- W2508968739
- Cited by
- 229
- References
- 54
- Citations by year
- 2026: 16 · 2025: 20 · 2024: 28 · 2023: 28 · 2022: 20 · 2021: 34 · 2020: 20 · 2019: 17 · 2018: 21 · 2017: 22 · 2016: 3
- FWCI
- 10.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (publishedVersion, other-oa)
- PubMed Central (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (R01AG011085)
- National Cancer Institute (P30CA021765)
- National Institute of General Medical Sciences (R37GM069530)
- National Institute of Diabetes and Digestive and Kidney Diseases (K01DK098285)
- National Institute of Neurological Disorders and Stroke (R37NS083524)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- Cullin-RING E3 ligases, monoubiquitylation, ubiquitin transfer, E2 ubiquitin ligase, polyubiquitination, proteostasis
- MeSH terms
- NEDD8 Protein, Carrier Proteins, Humans, Mutation, Substrate Specificity, Ubiquitins, Ubiquitin, Polyubiquitin, Proteomics, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Cullin Proteins, Ubiquitination, Gene Knockdown Techniques, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
