Structural assembly of cullin-RING ubiquitin ligase complexes
Open accessAbstract
The cullin-RING ubiquitin ligases (CRLs) are the largest family of multi-subunit E3 ligases in eukaryotes, which ubiquitinate protein substrates in numerous cellular pathways. CRLs share a common arched scaffold and a RING domain catalytic subunit, but use different adaptors and substrate receptors to assemble unique E3 machineries. In comparison to the first CRL structure, recent findings have revealed increased complexity in the overall architecture and assembly mode of CRLs, including multi-domain organization, inter-domain flexibility, and subunit dimerization. These features highlight the capacity of CRLs to catalyze protein ubiquitination under distinct cellular contexts and in response to diverse signals. As the first installment of a two-review series, this article will focus on recent advances in our understanding of CRL assembly mechanisms.
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?
CUL4 can rotate up to 150° around DDB1, generating a large ubiquitylation zone spacious enough to allow CRBN autoubiquitylation without a substrate being present.
“Structural studies show that cul4 can rotate up to 150° around DDB1, the cRBN adaptor, generating a large ubiquitylation zone spacious enough to allow cRBN autoubiquitylation without a substrate being present (Zimmerman et al. 2010;Fischer et al. 2014).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Zimmerman et al. 2010
The CRL4A E3 machinery section reports rotational flexibility within DDB1 and suggests that it could let a CRL4 complex sample a large area around a substrate complex. It does not give a 150° rotation, identify CRBN as the adaptor (it identifies DDB1), or say that this flexibility permits CRBN autoubiquitylation without a substrate. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCDK12 acts as a pseudo-substrate receptor which positions CycK within the expansive ubiquitylation zone of CRL4 ligases.
“cDK12 therefore acts as a pseudo-substrate receptor which positions cycK within the expansive ubiquitylation zone of cRl4 ligases (Zimmerman et al. 2010;Słabicki et al. 2020a).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Zimmerman et al. 2010
The section “CRL4A E3 machinery: mobile propellers and cryptic helices” (page not provided) says CRL4’s structural flexibility might let it sample a large area around a substrate complex. It does not identify CDK12 as a pseudo-substrate receptor or say that CDK12 positions CycK there. (LLM, conf=0.86)
Experimental — accuracy not yet measuredUbiquitin E3 ligases serve as scaffolds between a target protein and an activated E2-Ub, binding both and catalysing transfer of ubiquitin from the E2 active site cysteine to a lysine on the target.
“ubiquitin E3 ligases serve as scaffolds between a target protein and an activated ubiquitin E2 conjugating enzyme charged with a ubiquitin molecule (E2–Ub), by binding both molecules, then catalysing the transfer of ubiquitin from the active site cysteine of the E2 onto a lysine side chain of a target protein104–107.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [104]
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
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · see citing works
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · see citing works
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
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
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
SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544 · see citing works
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507 · see citing works
Self-citationZhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · 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
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084 · see citing works
Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade
Scheffner, M., Nuber, U. A., & Huibregtse, J. M. (1995) · Nature · doi:10.1038/373081a0 · Cited by 1,017 · see citing works
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
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
Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function
Stebbins, C. E., Kaelin, W. G., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.284.5413.455 · Cited by 852 · 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
Self-citationTsvetkov, L. M., Yeh, K., Lee, S.-J., Sun, H., & Zhang, H. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80290-5 · Cited by 791 · see citing works
Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
Nash, P., Tang, X., Orlicky, S. M., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T. J., & Tyers, M. (2001) · Nature · doi:10.1038/35107009 · Cited by 761 · see citing works
Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759 · see citing works
Furukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 746 · 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 · 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
Molecular architecture and assembly of the DDB1–CUL4A ubiquitin ligase machinery
Angers, S., Li, T., Yi, X., MacCoss, M. J., Moon, R. T., & Zheng, N. (2006) · Nature · doi:10.1038/nature05175 · Cited by 674 · see citing works
Self-citationJin, J., Arias, E. E., Chen, J., Harper, J. W., & Walter, J. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.010 · Cited by 632 · see citing works
Structure of a β-TrCP1-Skp1-β-Catenin Complex
Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612 · see citing works
Self-citationInsights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex
Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E., Finnin, M. S., Elledge, S. J., Harper, J. W., Pagano, M., & Pavletich, N. P. (2000) · Nature · doi:10.1038/35042620 · Cited by 610 · see citing works
Self-citationStructure 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
Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works
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
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
Self-citationKamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., & Nakayama, K. I. (2004) · Genes & Development · doi:10.1101/gad.1252404 · Cited by 476 · 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
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
Tong, K. I., Padmanabhan, B., Kobayashi, A., Shang, C., Hirotsu, Y., Yokoyama, S., & Yamamoto, M. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00753-07 · Cited by 447 · see citing works
Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex
Scrima, A., Koníčková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., & Thomä, N. H. (2008) · Cell · doi:10.1016/j.cell.2008.10.045 · Cited by 441 · 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
Higa, L. A., Wu, M., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1490 · Cited by 414 · 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
Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecules and Cells · Cited by 333 · see citing works
Self-citationDDB1 functions as a linker to recruit receptor WD40 proteins to CUL4–ROC1 ubiquitin ligasesPreprint
He, Y. J., McCall, C. M., Hu, J., Zeng, Y., & Xiong, Y. (2006) · Genes & Development · doi:10.1101/gad.1483206 · Cited by 331 · see citing works
Zachariae, W., Shevchenko, A., Andrews, P. D., Ciosk, R., Gálová, M., Stark, M. J. R., Mann, M., & Nasmyth, K. (1998) · Science · doi:10.1126/science.279.5354.1216 · Cited by 326 · see citing works
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
Mechanism of SMRT Corepressor Recruitment by the BCL6 BTB Domain
Ahmad, K. F., Melnick, A. M., Lax, S. A., Bouchard, D., Liu, J., Kiang, C. L., Mayer, S., Takahashi, S., Licht, J. D., & Privé, G. G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00454-4 · Cited by 282 · see citing works
Li, T., Chen, X., Garbutt, K. C., Zhou, P., & Zheng, N. (2006) · Cell · doi:10.1016/j.cell.2005.10.033 · Cited by 255 · see citing works
Self-citationCrystal Structure of the Kelch Domain of Human Keap1
Li, X., Zhang, D. D., Hannink, M., & Beamer, L. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410073200 · Cited by 249 · see citing works
Ogura, T., Tong, K. I., Mio, K., Maruyama, Y., Kurokawa, H., Sato, C., & Yamamoto, M. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914036107 · Cited by 232 · see citing works
Ulane, C. M., & Horvath, C. M. (2002) · Virology · doi:10.1006/viro.2002.1773 · Cited by 225 · see citing works
Li, T., Robert, E. I., Breugel, P. C. V., Strubin, M., & Zheng, N. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1719 · Cited by 223 · see citing works
Self-citationTang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209 · see citing works
Mahrour, N., Redwine, W. B., Florens, L., Swanson, S. K., Martin-Brown, S., Bradford, W. D., Staehling-Hampton, K., Washburn, M. P., Conaway, R. C., & Conaway, J. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706987200 · Cited by 196 · see citing works
Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundström, M., & Knapp, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601638103 · Cited by 165 · see citing works
Cullin 4A Associates with the UV-damaged DNA-binding Protein DDB
Shiyanov, P. A., Nag, A., & Raychaudhuri, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35309 · Cited by 159 · see citing works
UV-damaged DNA-binding Proteins Are Targets of CUL-4A-mediated Ubiquitination and Degradation
Chen, X., Zhang, Y., Douglas, L. C., & Zhou, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106808200 · Cited by 149 · see citing works
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
Fbw7/hCDC4 dimerization regulates its substrate interactions.
Welcker, M., & Clurman, B. E. (2007) · Cell Division · doi:10.1186/1747-1028-2-7 · Cited by 115 · see citing works
Ubiquitin proteasome system (UPS): what can chromatin do for you?
O’Connell, B. C., & Harper, J. W. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.014 · Cited by 115 · see citing works
PARC and CUL7 Form Atypical Cullin RING Ligase Complexes
Skaar, J. R., Florens, L. A., Tsutsumi, T., Arai, T., Tron, A. E., Swanson, S. K., Washburn, M. P., & DeCaprio, J. A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3241 · Cited by 77 · see citing works
DDB2 (damaged-DNA binding protein 2) in nucleotide excision repair and DNA damage response
Stoyanova, T., Roy, N., Kopanja, D., Raychaudhuri, P., & Bagchi, S. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10109 · Cited by 70 · see citing works
Chew, E., Poobalasingam, T., Hawkey, C. J., & Hagen, T. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.12.002 · Cited by 63 · see citing works
Dixon, C., Brunson, L. E., Roy, M. M., Smothers, D. B., Sehorn, M. G., & Mathias, N. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.1.123-133.2003 · Cited by 22 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [60]Hao B Oehlmann S Sowa ME Harper JW Pavletich NP Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases Molecular Cell 2007 26 131 143 17434132
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
Ubiquitin ligases: structure, function, and regulation
Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499 · see citing works
Integrated molecular analysis of clear-cell renal cell carcinoma
Sato, Y., Yoshizato, T., Shiraishi, Y., Maekawa, S., Okuno, Y., Kamura, T., Shimamura, T., Sato‐Otsubo, A., Nagae, G., Suzuki, H., et al. (2013) · Nature Genetics · doi:10.1038/ng.2699 · Cited by 1,223 · see citing works
Mechanisms and function of substrate recruitment by F-box proteins
Skaar, J. R., Pagan, J. K., & Pagano, M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3582 · Cited by 671 · see citing works
Advancing targeted protein degradation for cancer therapy
Dale, B., Cheng, M., Park, K., Kanıskan, H. Ü., Xiong, Y., & Jin, J. J. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00365-x · Cited by 671 · 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
Structural basis of Keap1 interactions with Nrf2
Canning, P., Sorrell, F. J., & Bullock, A. N. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.034 · Cited by 605 · see citing works
The Ubiquitin–Proteasome System of Saccharomyces cerevisiae
Finley, D. J., Ulrich, H. D., Sommer, T., & Kaiser, P. (2012) · Genetics · doi:10.1534/genetics.112.140467 · Cited by 427 · see citing works
The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 426 · see citing works
An expanded tool kit for the auxin‐inducible degron system in budding yeast
Morawska, M., & Ulrich, H. D. (2013) · Yeast · doi:10.1002/yea.2967 · Cited by 414 · see citing works
Delineating the role of cooperativity in the design of potent PROTACs for BTK
Zorba, A., Nguyen, C., Xu, Y., Starr, J., Borzilleri, K., Smith, J., Zhu, H., Farley, K. A., Ding, W., Schiemer, J., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803662115 · Cited by 419 · 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
“The Cullin subunit (Cul1–5 or Cul7) forms a central stalk-like scaffold that orients and constrains the substrate binding and catalytic centers (3, 4).”
Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237 · see citing works
Two 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-citationCrystal structure of the human COP9 signalosome
Lingaraju, G. M., Bunker, R. D., Cavadini, S., Heß, D., Hassiepen, U., Renatus, M., Fischer, E. S., & Thomä, N. H. (2014) · Nature · doi:10.1038/nature13566 · Cited by 231 · see citing works
Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15
Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., & Fischer, E. S. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0378-3 · Cited by 218 · see citing works
Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome
Cavadini, S., Fischer, E. S., Bunker, R. D., Potenza, A., Lingaraju, G. M., Goldie, K. N., Mohamed, W. I., Faty, M., Petzold, G., Beckwith, R. E. J., et al. (2016) · Nature · doi:10.1038/nature17416 · Cited by 213 · see citing works
Structural regulation of cullin-RING ubiquitin ligase complexes
Duda, D. M., Scott, D. C., Calabrese, M. F., Zimmerman, E. S., Zheng, N., & Schulman, B. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.01.003 · Cited by 205 · see citing works
Self-citationStructural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif
Guo, Y., Dong, L., Qiu, X., Wang, Y., Zhang, B., Liu, H., Yu, Y., Zang, Y., Yang, M., & Huang, Z. (2014) · Nature · doi:10.1038/nature12884 · 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-citationAhn, J., Hao, C., Yan, J., DeLucia, M., Mehrens, J., Wang, C., Gronenborn, A. M., & Skowroński, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.340711 · Cited by 186 · see citing works
CRL4B Catalyzes H2AK119 Monoubiquitination and Coordinates with PRC2 to Promote Tumorigenesis
Hu, H., Yang, Y., Ji, Q., Zhao, W., Jiang, B., Liu, R., Yuan, J., Liu, Q., Li, X., Zou, Y., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.024 · Cited by 185 · 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
Haven't got a glue: Protein surface variation for the design of molecular glue degraders
Kozicka, Z., & Thomä, N. H. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.04.009 · Cited by 170 · see citing works
Allo-network drugs: harnessing allostery in cellular networks
Nussinov, R., Tsai, C., & Csermely, P. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.08.004 · Cited by 143 · see citing works
Abbas, T., & Dutta, A. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14530 · Cited by 144 · see citing works
The Genetic and Biochemical Basis of FANCD2 Monoubiquitination
Rajendra, E., Oestergaard, V. H., Langevin, F., Wang, M., Dornan, G. L., Patel, K. J., & Passmore, L. A. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.001 · Cited by 128 · see citing works
The SOCS box—Adapting proteins for ubiquitination and proteasomal degradation
Linossi, E. M., & Nicholson, S. E. (2012) · IUBMB Life · doi:10.1002/iub.1011 · Cited by 122 · see citing works
Morimoto, K., Ohama, N., Kidokoro, S., Mizoi, J., Takahashi, F., Todaka, D., Mogami, J., Sato, H., Qin, F., Kim, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704189114 · Cited by 114 · see citing works
FANCD2–FANCI is a clamp stabilized on DNA by monoubiquitination of FANCD2 during DNA repair
Alcón, P., Shakeel, S., Chen, Z. A., Rappsilber, J., Patel, K. J., & Passmore, L. A. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0380-1 · Cited by 112 · see citing works
Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B
Hannah, J., & Zhou, P. (2015) · Gene · doi:10.1016/j.gene.2015.08.064 · Cited by 108 · see citing works
Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins
Shin, Y. J., Park, S. K., Jung, Y. J., Kim, Y. N., Kim, K. S., Park, O. K., Kwon, S., Jeon, S. H., Trinh, L. A., Fraser, S. E., et al. (2015) · Scientific Reports · doi:10.1038/srep14269 · Cited by 110 · see citing works
Nakagawa, T., & Xiong, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.033 · Cited by 107 · see citing works
Structure of the Fanconi anaemia monoubiquitin ligase complex
Shakeel, S., Rajendra, E., Alcón, P., O’Reilly, F. J., Chorev, D. S., Maslen, S., Degliesposti, G., Russo, C. J., He, S., Hill, C. H., et al. (2019) · Nature · doi:10.1038/s41586-019-1703-4 · Cited by 107 · see citing works
BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs
Mathew, R. S., Seiler, M. P., Scanlon, S. T., Mao, A., Constantinides, M. G., Bertozzi-Villa, C., Singer, J. D., & Bendelac, A. S. (2012) · Nature · doi:10.1038/nature11548 · Cited by 105 · see citing works
Small Rho GTPases in the control of cell shape and mobility
Murali, A., & Rajalingam, K. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1519-6 · Cited by 105 · see citing works
Modularized Functions of the Fanconi Anemia Core Complex
Huang, Y., Leung, J. W. C., Lowery, M. G., Matsushita, N., Wang, Y., Shen, X. H., Do, H., Takata, M., Chen, J., & Li, L. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.029 · Cited by 103 · see citing works
Cullin E3 Ligases and Their Rewiring by Viral Factors
Mahon, C., Krogan, N., Craik, C., & Pick, E. (2014) · Biomolecules · doi:10.3390/biom4040897 · Cited by 101 · see citing works
Brown, N. G., VanderLinden, R. T., Watson, E. R., Qiao, R., Grace, C. R., Yamaguchi, M., Weissmann, F., Frye, J. J., Dube, P., Cho, S. E., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504161112 · Cited by 97 · see citing works
Self-citationMotta, M., Fidan, M., Bellacchio, E., Pantaleoni, F., Schneider‐Heieck, K., Coppola, S., Borck, G., Salviati, L., Zenker, M., Cirstea, I. C., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy412 · Cited by 101 · see citing works
Recognition of the Diglycine C-End Degron by CRL2KLHDC2 Ubiquitin Ligase
Rusnac, D.-V., Lin, H.-C., Canzani, D., Tien, K. X., Hinds, T. R., Tsue, A. F., Bush, M. F., Yen, H.-C. S., & Zheng, N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.021 · Cited by 93 · see citing works
“The BC-box protein KLHDC2 contains a C-terminal region responsible for CUL2-Elongin-B/C binding and an N-terminal kelch repeat β-propeller domain, which is commonly used by CRL substrate receptor subunits to engage substrates (Duda et al., 2011; Mahrour et al., 2008; Zimmerman et al., 2010).”
Self-citationCullin-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
Phototropism: Translating light into directional growth
Hohm, T., Preuten, T., & Fankhauser, C. (2012) · American Journal of Botany · doi:10.3732/ajb.1200299 · Cited by 91 · see citing works
Duda, D. M., Olszewski, J. L., Tron, A. E., Hammel, M., Lambert, L. J., Waddell, M. B., Mittag, T., DeCaprio, J. A., & Schulman, B. A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.044 · Cited by 90 · see citing works
Self-citationNEDD8 — 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
Jasmonate perception: Ligand–receptor interaction, regulation, and evolution
Hu, S., Yu, K., Yan, J., Shan, X., & Xie, D. (2022) · Molecular Plant · doi:10.1016/j.molp.2022.08.011 · Cited by 85 · 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-citationThe ubiquitin–proteasome system as a transcriptional regulator of plant immunity
Adams, E. H. G., & Spoel, S. H. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery216 · Cited by 79 · see citing works
Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms
Chen, Z., Sui, J., Zhang, F., & Zhang, C. (2015) · Journal of Cancer · doi:10.7150/jca.11076 · Cited by 79 · see citing works
The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions
Cai, W., & Yang, H. (2016) · Cell Division · doi:10.1186/s13008-016-0020-7 · Cited by 80 · see citing works
Mechanisms of Translation-coupled Quality Control
Inada, T., & Beckmann, R. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168496 · Cited by 72 · see citing works
Disease‐causing mutations in KLHL3 impair its effect on WNK4 degradation
Wu, G., & Peng, J. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.032 · Cited by 76 · see citing works
The ubiquitin ligase adaptor SPOP in cancer
Cuneo, M. J., & Mittag, T. (2019) · FEBS Journal · doi:10.1111/febs.15056 · Cited by 74 · see citing works
The ubiquitin proteasome system and myocardial ischemia
Calise, J., & Powell, S. R. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00604.2012 · Cited by 70 · see citing works
Mechanism of immunomodulatory drugs' action in the treatment of multiple myeloma
Chang, X.-B., Zhu, Y., Shi, C., & Stewart, A. K. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt142 · Cited by 69 · see citing works
Ubiquitin and Parkinson's disease through the looking glass of genetics
Walden, H., & Muqit, M. M. K. (2017) · Biochemical Journal · doi:10.1042/bcj20160498 · Cited by 67 · see citing works
The Molecular Genetics of Gordon Syndrome
Mabillard, H. R., & Sayer, J. A. (2019) · Genes · doi:10.3390/genes10120986 · Cited by 68 · see citing works
Chen, Z., Zhang, W., Jiang, K., Chen, B., Wang, K., Lao, L., Hou, C., Wang, F., Zhang, C., & Shen, H. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.12.010 · Cited by 66 · see citing works
Zhang, Y., Shi, Z., Zhou, Y., Xiao, Q., Wang, H., & Peng, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01865 · Cited by 67 · see citing works
Specificity and disease in the ubiquitin system
Chaugule, V. K., & Walden, H. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150209 · Cited by 62 · see citing works
Chen, Y.-A., Peng, Y.-J., Hu, M.-C., Huang, J.-J., Chien, Y.-C., Wu, J.-T., Chen, T.-Y., & Tang, C.-Y. (2015) · Scientific Reports · doi:10.1038/srep10667 · Cited by 61 · see citing works
Yu, J. J., Lan, X., Chen, X., Yu, C. Y., Xu, Y., Liu, Y., Xu, L., Fan, H., & Tong, C. (2016) · Development · doi:10.1242/dev.134247 · Cited by 60 · see citing works
Macromolecular juggling by ubiquitylation enzymes
Lorenz, S., Cantor, A. J., Rapé, M., & Kuriyan, J. (2013) · BMC Biology · doi:10.1186/1741-7007-11-65 · Cited by 57 · see citing works
Selective Recruitment of an E2∼Ubiquitin Complex by an E3 Ubiquitin Ligase
Spratt, D. E., Wu, K., Kovacev, J., Pan, Z., & Shaw, G. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.353748 · Cited by 59 · see citing works
Jang, S., Redon, C. E., & Aladjem, M. I. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00019 · Cited by 56 · see citing works
Samant, R. S., Clarke, P. A., & Workman, P. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322412111 · Cited by 55 · see citing works
Schwefel, D., Boucherit, V., Christodoulou, E., Walker, P. A., Stoye, J. P., Bishop, K. N., & Taylor, I. A. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.03.004 · Cited by 53 · see citing works
Li, Y., Jin, K., Bunker, E. N., Zhang, X., Luo, X., Liu, X., & Hao, B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708677115 · Cited by 53 · see citing works
Flexible Cullins in Cullin-RING E3 Ligases Allosterically Regulate Ubiquitination
Liu, J., & Nussinov, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277236 · Cited by 52 · see citing works
Ullah, K., Zubia, E., Narayan, M., Yang, J., & Xu, G. (2018) · FEBS Journal · doi:10.1111/febs.14708 · Cited by 51 · see citing works
Nie, L., Zhao, Y., Wu, W., Yang, Y.-Z., Wang, H.-C., & Sun, X.-H. (2010) · Cell Research · doi:10.1038/cr.2010.165 · Cited by 50 · see citing works
Spatial organization of ubiquitin ligase pathways orchestrates neuronal connectivity
Yamada, T., Yang, Y., & Bonni, A. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2012.12.004 · Cited by 48 · see citing works
Zhang, C., Chen, B., Jiang, K., Lao, L., Shen, H., & Chen, Z. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12176 · Cited by 49 · see citing works
Off the beaten paths: alternative and crosstalk regulation of Rho GTPases
Boulter, E., Estrach, S., García‐Mata, R., & Féral, C. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-192252 · Cited by 47 · see citing works
Andresen, C. A., Smedegaard, S. B., Sylvestersen, K. B., Svensson, C., Iglesias‐Gato, D., Cazzamali, G., Nielsen, T. K., Nielsen, M. L., & Flores‐Morales, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.534602 · Cited by 47 · see citing works
FBXO32, encoding a member of the SCF complex, is mutated in dilated cardiomyopathy
Al‐Yacoub, N., Shaheen, R., Awad, S. M., Kunhi, M., Dzimiri, N., Nguyen, H. C., Xiong, Y., Alburaiki, J., AlHabeeb, W., Alkuraya, F. S., et al. (2016) · Genome biology · doi:10.1186/s13059-015-0861-4 · Cited by 46 · see citing works
Yasukawa, T., Tsutsui, A., Tomomori‐Sato, C., Sato, S., Saraf, A., Washburn, M. P., Florens, L. A., Terada, T., Shimizu, K., Conaway, R., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.059 · Cited by 43 · see citing works
Calabrese, M. F., Scott, D. C., Duda, D. M., Grace, C. R., Kurinov, I. V., Kriwacki, R. W., & Schulman, B. A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2086 · Cited by 45 · see citing works
Self-citationXu, Q., Hou, Y.-X., Langlais, P. R., Erickson, P. W., Zhu, J. J., Shi, C.-X., Luo, M., Zhu, Y., Xu, Y., Mandarino, L. J., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2331-0 · Cited by 45 · see citing works
HPV Oncoproteins and the Ubiquitin Proteasome System: A Signature of Malignancy?
Đukić, A., Lulić, L., Thomas, M., Skelin, J., Saidu, N. E. B., Grce, M., Banks, L., & Tomaić, V. (2020) · Pathogens · doi:10.3390/pathogens9020133 · Cited by 46 · 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
Self-citationDiscovery of Novel Pyrazolo-pyridone DCN1 Inhibitors Controlling Cullin Neddylation
Kim, H. S., Hammill, J. T., Scott, D. C., Chen, Y., Min, J., Rector, J., Singh, B., Schulman, B. A., & Guy, R. K. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00410 · Cited by 43 · see citing works
Self-citationCRL Ubiquitin Ligases and DNA Damage Response
Li, J.-M., & Jin, J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00029 · Cited by 41 · see citing works
DCAF13 promotes breast cancer cell proliferation by ubiquitin inhibiting PERP expression
Shan, B., Wang, X., Zheng, L., Yao, H., Gao, J., Lv, M., Zhang, Y., Liu, Y., Zhang, H., Chen, H., et al. (2022) · Cancer Science · doi:10.1111/cas.15300 · Cited by 42 · see citing works
Zhang, C., Cheng, Q., Wang, H., Gao, H., Fang, X. D., Chen, X., Zhao, M., Wei, W., Song, B., Liu, S., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01907-7 · Cited by 40 · see citing works
Kim, Y. K., Kwak, M., Ku, B., Suh, H., Joo, K., Lee, J., Jung, J. U., & Oh, B. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913011220 · Cited by 41 · see citing works
Single-particle EM reveals extensive conformational variability of the Ltn1 E3 ligase
Lyumkis, D., Doamekpor, S. K., Bengtson, M. H., Lee, J., Toro, T. B., Petroski, M. D., Lima, C. D., Potter, C. S., Carragher, B. O., & Joazeiro, C. A. P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210041110 · Cited by 40 · see citing works
SPLINTS: small-molecule protein ligand interface stabilizers
Fischer, E. S., Park, E., Eck, M. J., & Thomä, N. H. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.01.004 · Cited by 39 · see citing works
Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP
van Geersdaele, L. K., Stead, M., Harrison, C. M., Carr, S. B., Close, H. J., Rosbrook, G. O., Connell, S. D., & Wright, S. C. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913012687 · Cited by 39 · see citing works
New insights into the function of Cullin 3 in trophoblast invasion and migration
Zhang, Q., Song, Y., Huang, X., Tan, Y., Zhu, C., Wang, Y., Wang, H., Lin, H., Fu, J., & Wang, H. (2015) · Reproduction · doi:10.1530/rep-15-0126 · Cited by 38 · see citing works
Interactions of Bacterial Proteins with Host Eukaryotic Ubiquitin Pathways
Perrett, C. A., Lin, D. Y.-W., & Zhou, D. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00143 · Cited by 37 · see citing works
Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway
Bhowmick, P., Pancsa, R., Guharoy, M., & Tompa, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065443 · Cited by 36 · see citing works
Signal-Induced Disassembly of the SCF Ubiquitin Ligase Complex by Cdc48/p97
Yen, J. L., Flick, K. M., Papagiannis, C. V., Mathur, R., Tyrrell, A., Ouni, I., Kaake, R. M., Huang, L., & Kaiser, P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.015 · Cited by 37 · see citing works
SCFFbxw5 mediates transient degradation of actin remodeller Eps8 to allow proper mitotic progression
Werner, A. A., Disanza, A., Reifenberger, N., Habeck, G., Becker, J., Calabrese, M. F., Urlaub, H., Lorenz, H., Schulman, B. A., Scita, G., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2661 · Cited by 34 · see citing works
Self-citationMolecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases
Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.06.015 · Cited by 34 · see citing works
SAMHD1 … and Viral Ways around It
Deutschmann, J., & Gramberg, T. (2021) · Viruses · doi:10.3390/v13030395 · Cited by 31 · see citing works
Cullin 3, a cellular scripter of the non-proteolytic ubiquitin code
Jerabkova, K., & Sumara, I. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.12.007 · Cited by 33 · see citing works
FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends on a Cullin 4B/DDB1 Complex
Sjögren, B., Swaney, S. M., & Neubig, R. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123581 · Cited by 33 · see citing works
Hörer, S., Reinert, D. J., Ostmann, K., Hoevels, Y., & Nar, H. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430911301124x · Cited by 32 · see citing works
Clinical and Molecular Perspectives of Monogenic Hypertension
Levanovich, P., Diaczok, A., & Rossi, N. F. (2019) · Current Hypertension Reviews · doi:10.2174/1573402115666190409115330 · Cited by 31 · see citing works
- Authors
- Zimmerman, E. S., Schulman, B. A., & Zheng, N.
- Affiliations
- University of Washington (US)
- St. Jude Children's Research Hospital (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Zheng, Ning
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 20
- Issue
- 6
- Pages
- 714-721
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC3070871
- OpenAlex
- W2029890158
- Cited by
- 227
- References
- 62
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 12 · 2023: 11 · 2022: 14 · 2021: 14 · 2020: 15 · 2019: 18 · 2018: 13 · 2017: 12 · 2016: 17 · 2015: 18 · 2014: 14 · 2013: 21 · 2012: 17
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (R01CA107134)
- National Institute of General Medical Sciences (F32GM093497, R01GM069530)
- 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
- cullin-RING ubiquitin ligases, E3 ubiquitin ligase, ubiquitination, RING domain, adaptor proteins, substrate receptor, subunit dimerization
- MeSH terms
- Animals, Humans, Protein Structure, Secondary, Protein Structure, Quaternary, Ubiquitin-Protein Ligases, F-Box Proteins, Protein Multimerization
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
