Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1
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RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar yet mechanistically distinct from canonical RING domains. Both types of E3 bind E2∼ubiquitin (E2∼Ub) via their RINGs but canonical RING E3s promote closed E2∼Ub conformations required for direct Ub transfer from the E2 to substrate, while RBR RING1s promote open E2∼Ub to favor Ub transfer to the E3 active site. This different RING/E2∼Ub conformation determines its direct target, which for canonical RING E3s is typically a substrate or substrate-linked Ub, but is the E3 active-site cysteine in the case of RBR-type E3s. Here we show that a short extension of HHARI RING1, namely Zn 2+ -loop II, not present in any RING E3s, acts as a steric wedge to disrupt closed E2∼Ub, providing a structural explanation for the distinctive RING1-dependent conformational restriction mechanism utilized by RBR E3s.
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RBR ligases use a hybrid between the RING and HECT ligation strategies.
“RBR ligases use a hybrid between the RING and HECT ligation strategies114,115.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [115]
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Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works
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 15,720 · see citing works
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,671 · see citing works
<i>MolProbity</i> : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
NMR View: A computer program for the visualization and analysis of NMR data
Johnson, B. A., & Blevins, R. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404272 · Cited by 3,093 · see citing works
Experimental phasing with SHELXC/D/E: combining chain tracing with density modification
Sheldrick, G. M. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909038360 · Cited by 1,093 · see citing works
Structure of a c-Cbl–UbcH7 Complex
Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839 · 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
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
Self-citationUBCH7 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
Self-citationStructure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
Trempe, J.-F., Sauvé, V., Grenier, K., Seirafi, M., Tang, M. Y. H., Ménade, M., Al-Abdul-Wahid, S., Krett, J. D., Wong, K. T. K., Kozlov, G., et al. (2013) · Science · doi:10.1126/science.1237908 · Cited by 549 · see citing works
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521 · see citing works
Kim, H. T., Kim, K. P., Lledı́as, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., Gygi, S. P., & Goldberg, A. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609659200 · Cited by 438 · see citing works
Energetics of hydrogen bonds in peptides
Sheu, S., Yang, D., Selzle, H. L., & Schlag, E. W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2133366100 · Cited by 379 · see citing works
Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T. A., Walker, D., Yang, Y., Regnström, K. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2982 · Cited by 368 · see citing works
E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages
Christensen, D. E., Brzovic, P. S., & Klevit, R. E. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1295 · Cited by 351 · see citing works
Self-citationBinding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex
Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346 · see citing works
Self-citationStructure of the human Parkin ligase domain in an autoinhibited state
Wauer, T., & Komander, D. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.125 · Cited by 334 · see citing works
Structure of an E3:E2∼Ub Complex Reveals an Allosteric Mechanism Shared among RING/U-box Ligases
Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., & Klevit, R. E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.001 · Cited by 333 · see citing works
Self-citationBIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2379 · Cited by 319 · see citing works
RBR E3 ubiquitin ligases: new structures, new insights, new questions
Spratt, D. E., Walden, H., & Shaw, G. S. (2014) · Biochemical Journal · doi:10.1042/bj20140006 · Cited by 314 · see citing works
Insights into Ubiquitin Transfer Cascades from a Structure of a UbcH5B∼Ubiquitin-HECTNEDD4L Complex
Kamadurai, H., Souphron, J., Scott, D. C., Duda, D. M., Miller, D. J., Stringer, D. K., Piper, R. C., & Schulman, B. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.010 · Cited by 292 · see citing works
Self-citationGoldenberg, S. J., Cascio, T. C., Shumway, S. D., Garbutt, K. C., Liu, J., Xiong, Y., & Zheng, N. (2004) · Cell · doi:10.1016/j.cell.2004.10.019 · Cited by 280 · see citing works
Super-resolution biomolecular crystallography with low-resolution data
Schroeder, G. F., Levitt, M., & Brünger, A. T. (2010) · Nature · doi:10.1038/nature08892 · Cited by 269 · see citing works
Polyubiquitination by HECT E3s and the Determinants of Chain Type Specificity
Kim, H. C., & Huibregtse, J. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00240-09 · Cited by 252 · 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
Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal
DaRosa, P. A., Wang, Z., Jiang, X., Pruneda, J. N., Cong, F., Klevit, R. E., & Xu, W. (2014) · Nature · doi:10.1038/nature13826 · Cited by 230 · see citing works
Self-citationTwo Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.027 · Cited by 229 · see citing works
Self-citationLUBAC synthesizes linear ubiquitin chains via a thioester intermediate
Stieglitz, B., Morris-Davies, A. C., Koliopoulos, M. G., Christodoulou, E., & Rittinger, K. (2012) · EMBO Reports · doi:10.1038/embor.2012.105 · Cited by 220 · see citing works
Self-citationSmit, J. J., Monteferrario, D., Noordermeer, S. M., van Dijk, W. J., van der Reijden, B. A., & Sixma, T. K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.217 · Cited by 210 · 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
Self-citationScott, 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-citationFunctional role of TRIM E3 ligase oligomerization and regulation of catalytic activity
Koliopoulos, M. G., Esposito, D., Christodoulou, E., Taylor, I. A., & Rittinger, K. (2016) · The EMBO Journal · doi:10.15252/embj.201593741 · Cited by 180 · see citing works
Self-citationSystem-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes
Zhang, W., Wu, K.-P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.005 · Cited by 168 · see citing works
Self-citationDas, R., Mariano, J. M., Tsai, Y. C., Kalathur, R., Kostova, Z., Li, J., Tarasov, S. G., McFeeters, R. L., Altieri, A. S., Ji, X., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.010 · Cited by 160 · 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-citationUbiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate
Pruneda, J. N., Stoll, K. E., Bolton, L. J., Brzović, P. S., & Klevit, R. E. (2011) · Biochemistry · doi:10.1021/bi101913m · Cited by 138 · see citing works
Self-citationEssentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. C. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2621 · Cited by 136 · see citing works
Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis
Wang, M., & Pickart, C. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600895 · Cited by 134 · see citing works
Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
Xu, Z., Kohli, E., Devlin, K. I., Bold, M. S., Nix, J. C., & Misra, S. (2008) · BMC Structural Biology · doi:10.1186/1472-6807-8-26 · Cited by 124 · see citing works
The ring between ring fingers (RBR) protein family
Eisenhaber, B., Chumak, N., Eisenhaber, F., & Hauser, M. (2007) · Genome biology · doi:10.1186/gb-2007-8-3-209 · Cited by 119 · see citing works
Ness, S. R., Graaff, R. A. G. D., Abrahams, J. P., & Pannu, N. S. (2004) · Structure · doi:10.1016/j.str.2004.07.018 · Cited by 118 · see citing works
Brown, N. G., Watson, E. R., Weissmann, F., Jarvis, M. A., VanderLinden, R. T., Grace, C. R., Frye, J. J., Qiao, R., Dube, P., Petzold, G., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.009 · Cited by 112 · see citing works
Self-citationTRIAD1 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-citationMolecular 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
Self-citationMolecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase
Wang, M., Cheng, D., Peng, J., & Pickart, C. M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601061 · Cited by 92 · see citing works
Haddad, D., Vilain, S., Vos, M. H., Esposito, G., Matta, S., Kalscheuer, V. M., Craessaerts, K., Leyssen, M., Nascimento, R. M. P., Vianna‐Morgante, A. M., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.012 · Cited by 89 · see citing works
Select E2 enzymes differentially regulate parkin activation and mitophagy
Fiesel, F. C., Moussaud-Lamodière, E. L., Ando, M., & Springer, W. (2014) · Journal of Cell Science · doi:10.1242/jcs.147520 · Cited by 72 · see citing works
High-Yield Expression in Escherichia coli and Purification of Mouse Ubiquitin-Activating Enzyme E1
Carvalho, A. F., Pinto, M. P., Grou, C. P. O., Vitorino, R. M. P., Domingues, P. M., Yamao, F., Sá-Miranda, C., & Azevedo, J. E. (2011) · Molecular Biotechnology · doi:10.1007/s12033-011-9463-x · Cited by 53 · see citing works
Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B
Li, S., Liang, Y., Mariano, J. M., Metzger, M. B., Stringer, D. K., Hristova, V. A., Li, J., Randazzo, P. A., Tsai, Y. C., Ji, X., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685867 · Cited by 37 · see citing works
Proteasome Inhibition Promotes Parkin-Ubc13 Interaction and Lysine 63-Linked Ubiquitination
Lim, G. G. Y., Chew, K. C. M., Ng, X., Basil, A. H., Sim, R. W. X., Tan, J. M. M., Chai, C., & Lim, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073235 · Cited by 28 · see citing works
Solution Structure of the RING finger Domain of the human UbcM4-interacting Protein 4
Miyamoto, Κ., Saito, K., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S., & Initiative, P. (2004) · Worldwide Protein Data Bank · doi:10.2210/pdb1wim/pdb · Cited by 1 · see citing works
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Self-citationVinci, M., Treccarichi, S., Rando, R. G., Musumeci, A., Todaro, V., Federico, C., Saccone, S., Elia, M., & Calı̀, F. (2024) · Scientific Reports · doi:10.1038/s41598-024-66475-2 · Cited by 22 · see citing works
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Boamah, D., Lin, T., Poppinga, F. A., Basu, S., Rahman, S., Essel, F., & Chakravarty, S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00705 · Cited by 21 · see citing works
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Martino, L., Brown, N. R., Masino, L., Esposito, D., & Rittinger, K. (2018) · Scientific Reports · doi:10.1038/s41598-017-18513-5 · Cited by 21 · see citing works
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Reiter, K. H., & Klevit, R. E. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8706-1_1 · Cited by 20 · see citing works
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Mauro, D., Manou-Stathopoulou, S., Rivellese, F., Sciacca, E., Goldmann, K., Tsang, V., Lucey-Clayton, I., Pagani, S., Alam, F., Pyne, D., et al. (2023) · Journal of Autoimmunity · doi:10.1016/j.jaut.2023.103023 · Cited by 20 · see citing works
Cullin-independent recognition of HHARI substrates by a dynamic RBR catalytic domain
Reiter, K. H., Zelter, A., Janowska, M. K., Riffle, M. E., Shulman, N., MacLean, B., Tamura, K., Chambers, M., MacCoss, M. J., Davis, T. N., et al. (2022) · Structure · doi:10.1016/j.str.2022.05.017 · Cited by 15 · see citing works
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Connelly, E. M., Rintala‐Dempsey, A. C., Gundogdu, M., Freeman, E. A., Koszela, J., Aguirre, J. D., Zhu, G., Kämäräinen, O., Tadayon, R., Walden, H., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403114121 · Cited by 13 · see citing works
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Cook, B. W., Lacoursiere, R. E., & Shaw, G. S. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.02.012 · Cited by 12 · see citing works
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Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase
Purser, N., Tripathi‐Giesgen, I., Li, J., Scott, D. C., Horn‐Ghetko, D., Baek, K., Schulman, B. A., Alpi, A. F., & Kleiger, G. (2023) · Biochemical Journal · doi:10.1042/bcj20230373 · Cited by 11 · see citing works
Self-citationBudhidarmo, R., Zhu, J., Middleton, A. J., & Day, C. L. (2018) · FEBS Letters · doi:10.1002/1873-3468.13029 · Cited by 11 · see citing works
Hayashida, R., Kikuchi, R., Imai, K., Kojima, W., Yamada, T., Iijima, M., Sesaki, H., Tanaka, K., Matsuda, N., & Yamano, K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102822 · Cited by 10 · see citing works
Structural basis for the pathogenicity of parkin catalytic domain mutants
Wagner, J. P., Sauvé, V., Saran, A., & Gehring, K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108051 · Cited by 9 · see citing works
Cheng, P., Hou, Y., Bian, M., Fang, X., Liu, Y., Rao, Y., Cao, S., Liu, Y., Zhang, S., Chen, Y., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-05650-z · Cited by 9 · see citing works
Streich, F. C., & Lima, C. D. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8706-1_12 · Cited by 6 · see citing works
ZNFX1 uses two-component ubiquitin circuitry to quarantine viral RNA
Squair, D. R., Rivers, E., Sowar, H., Balci, A., Harmo, R., Wright, D. J., Beniwal, G., Soetens, M., Mathur, S., Tollervey, A., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.02.015 · Cited by 5 · see citing works
Molecular mechanisms of PINK1/Parkin-mediated mitochondrial quality control
Bayne, A. N., & Trempe, J. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.014 · Cited by 5 · see citing works
Regulation of germ cell development by ARI1 family ubiquitin ligases in C. elegans
Poush, J. A., Blouin, N. A., Bona, K. R. D., Lažetić, V., & Fay, D. S. (2018) · Scientific Reports · doi:10.1038/s41598-018-35691-y · Cited by 5 · see citing works
Complex Conformational Interplay for Parkin Activation is Revealed by 19F NMR Spectroscopy
Connelly, E. M., & Shaw, G. S. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169397 · Cited by 4 · see citing works
Characterisation of HOIP RBR E3 ligase conformational dynamics using integrative modelling
Kausas, M., Esposito, D., Rittinger, K., & Fraternali, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-18890-6 · Cited by 4 · see citing works
Self-citationHua, X., Guo, Y., Li, P., Wang, Y., Han, X., Chen, J., Li, J., Chu, G.-C., Shi, J., Liu, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70054-6 · Cited by 3 · see citing works
E2 Partner Tunes the Ubiquitylation Specificity of Arkadia E3 Ubiquitin Ligase
Delegkou, G. N., Birkou, M., Fragkaki, N., Toro, T., Marousis, K. D., Episkopou, V., & Spyroulias, G. A. (2023) · Cancers · doi:10.3390/cancers15041040 · Cited by 3 · see citing works
Tools for the discovery of biopolymer producing cysteine relays
Mabbitt, P. D. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00792-y · Cited by 2 · see citing works
RBR Ubiquitin Transfer: Not Simply an “Open” and “Closed” Case?
Dunkerley, K. M., & Shaw, G. S. (2017) · Structure · doi:10.1016/j.str.2017.05.013 · Cited by 2 · see citing works
Review of the Structural Basis of Human E2 Conjugating Enzymes in Complexed with RING E3 Ligases
Gladu, E., Sayed, I., & Massiah, M. A. (2022) · Biochemistry · doi:10.5772/intechopen.101484 · Cited by 1 · see citing works
E3-mediated Ubiquitin and Ubiquitin-like Protein Ligation: Mechanisms and Chemical Probes
Krist, D. T., & Schulman, B. A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160691-00184
Self-citation
- Authors
- 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.
- Affiliations
- University of Washington (US)
- St. Jude Children's Research Hospital (US)
- The Francis Crick Institute (GB)
- Corresponding author
- Schulman, Brenda A.
- Klevit, Rachel E.
- ORCID
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 25
- Issue
- 6
- Pages
- 890-900.e5
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC5462532
- OpenAlex
- W2617774976
- Cited by
- 52
- References
- 58
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 4 · 2023: 6 · 2022: 6 · 2021: 7 · 2020: 7 · 2019: 3 · 2018: 10 · 2017: 5
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Structure (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Wellcome Trust (PHS\u00A0NRSA 5T32 GM007270)
- U.S. Department of Energy (DE-AC02-06CH11357)
- Cancer Research UK (FC001142)
- Howard Hughes Medical Institute (P41GM103403)
- American Pain Society
- National Institute of General Medical Sciences (R01 GM088055)
- National Institutes of Health (S10 RR029205, P30CA021765, R37GM069530)
- Medical Research Council
- Francis Crick Institute
- American Lebanese Syrian Associated Charities
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- UbcH7, RBR E3 ubiquitin ligase, ubiquitination, protein structure
- MeSH terms
- Protein Domains, Binding Sites, Carrier Proteins, Humans, Models, Molecular, Protein Conformation, Zinc, Crystallography, X-Ray, Catalytic Domain, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
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