The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade
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Huibregtse, J. M., Scheffner, M., & Howley, P. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04990.x · Cited by 879
Self-citation
Cited by
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
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
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951
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
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273
Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234
Building ubiquitin chains: E2 enzymes at work
Ye, Y., & Rape, M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2780 · Cited by 989
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Ravi, R., Mookerjee, B., Bhujwalla, Z. M., Sutter, C. H., Artemov, D., Zeng, Q., Dillehay, L. E., Madan, A., Semenza, G. L., & Bedi, A. (2000) · Genes & Development · doi:10.1101/gad.14.1.34 · Cited by 967
Jiang, Y.-H., Armstrong, D., Albrecht, U., Atkins, C. M., Noebels, J. L., Eichele, G., Sweatt, J. D., & Beaudet, A. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)80596-6 · Cited by 852
The N-end rule: functions, mysteries, uses
Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859
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
Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588
Ubiquitin, cellular inclusions and their role in neurodegeneration
Alves-Rodrigues, A., Gregori, L., & Figueiredo-Pereira, M. E. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01276-4 · Cited by 393
Topoisomerase inhibitors unsilence the dormant allele of Ube3a in neurons
Huang, H.-S., Allen, J. A., Mabb, A. M., King, I. F., Miriyala, J., Taylor-Blake, B., Sciaky, N., Dutton, J. W., Lee, H.-M., Chen, X., et al. (2012) · Nature · doi:10.1038/nature10726 · Cited by 387
Nakagawa, S., & Huibregtse, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.21.8244-8253.2000 · Cited by 382
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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
Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
Kamadurai, H. B., Qiu, Y., Deng, A., Harrison, J. S., MacDonald, C., Actis, M., Rodrigues, P., Miller, D. J., Souphron, J., Lewis, S. M., et al. (2013) · eLife · doi:10.7554/elife.00828 · Cited by 165
Liu, Y., Chen, J. J., Gao, Q., Dalal, S., Hong, Y., Mansur, C. P., Band, V., & Androphy, E. J. (1999) · Journal of Virology · doi:10.1128/jvi.73.9.7297-7307.1999 · Cited by 165
Glenn, C. (1997) · Molecular Human Reproduction · doi:10.1093/molehr/3.4.321 · Cited by 145
JESPERSEN, T., MEMBREZ, M., NICOLAS, C., PITARD, B., STAUB, O., OLESEN, S., BARO, I., & ABRIEL, H. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.01.008 · Cited by 138
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., & Schulman, B. A. (2013) · Structure · doi:10.1016/j.str.2013.04.019 · Cited by 128
Zanier, K., ould M'hamed ould Sidi, A., Boulade-Ladame, C., Rybin, V., Chappelle, A., Atkinson, A., Kieffer, B., & Travé, G. (2012) · Structure · doi:10.1016/j.str.2012.02.001 · Cited by 125
Liu, X., Yuan, H., Fu, B., Disbrow, G. L., Apolinario, T., Tomaić, V., Kelley, M. L., Baker, C. C., Huibregtse, J., & Schlegel, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410343200 · Cited by 99
Self-citationAn affinity-directed protein missile system for targeted proteolysis
Fulcher, L. J., Macartney, T., Bozatzi, P., Hornberger, A., Rojas-Fernandez, A., & Sapkota, G. P. (2016) · Open Biology · doi:10.1098/rsob.160255 · Cited by 91
Targeting endogenous proteins for degradation through the affinity-directed protein missile system
Fulcher, L. J., Hutchinson, L. D., Macartney, T. J., Turnbull, C., & Sapkota, G. P. (2017) · Open Biology · doi:10.1098/rsob.170066 · Cited by 79
Kuballa, P., Matentzoglu, K., & Scheffner, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m605117200 · Cited by 55
Self-citationPSMC5 insufficiency and P320R mutation impair proteasome function
Yu, Z.-Q., Carmichael, J., Collins, G. A., D'Agostino, M. D., Lessard, M., Firth, H. V., Harijan, P., Fry, A. E., Dean, J., Zhang, J., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae085 · Cited by 4
“The ubiquitination serves as a recognition signal enabling the substrate to be degraded by the 26S proteasome [1, 2].”
Metadata
- Authors
- Scheffner, M., Nuber, U., & Huibregtse, J. M.
- Venue
- Nature
- Published
- 1995-01
- Volume
- 373
- Issue
- 6509
- Pages
- 81-83
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2008044453
- Cited by
- 1,016
- References
- 1
- FWCI
- 16.82
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
