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Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
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Genomic Instability in Mice Lacking Histone H2AX
Celeste, A., Petersen, S., Romanienko, P. J., Fernandez-Capetillo, O., Chen, H. T., Sedelnikova, O. A., Reina-San-Martin, B., Coppola, V., Meffre, E., Difilippantonio, M. J., et al. (2002) · Science · doi:10.1126/science.1069398 · Cited by 1,385
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Interaction of the Fanconi Anemia Proteins and BRCA1 in a Common Pathway
Garcia-Higuera, I., Taniguchi, T., Ganesan, S., Meyn, M. S., Timmers, C., Hejna, J., Grompe, M., & D'Andrea, A. D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00173-3 · Cited by 1,198
Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., & Ohta, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000881200 · Cited by 634
Paull, T. T., Cortez, D., Bowers, B., Elledge, S. J., & Gellert, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111125998 · Cited by 282
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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
Interaction of Human DNA Polymerase η with Monoubiquitinated PCNA
Kannouche, P. L., Wing, J., & Lehmann, A. R. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00259-x · Cited by 845
Bott, M., Brevet, M., Taylor, B. S., Shimizu, S., Ito, T., Wang, L., Creaney, J., Lake, R. A., Zakowski, M. F., Reva, B., et al. (2011) · Nature Genetics · doi:10.1038/ng.855 · Cited by 717
Carbone, M., Yang, H., Pass, H. I., Krausz, T., Testa, J. R., & Gaudino, G. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3459 · Cited by 590
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
Morris, J. R., Boutell, C., Keppler, M., Densham, R., Weekes, D., Alamshah, A., Butler, L., Galanty, Y., Pangon, L., Kiuchi, T., et al. (2009) · Nature · doi:10.1038/nature08593 · Cited by 375
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
de Bie, P., & Ciechanover, A. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.16 · Cited by 296
The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1
Machida, Y. J., Machida, Y., Vashisht, A. A., Wohlschlegel, J. A., & Dutta, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.046755 · Cited by 274
FANCJ Is a Structure-specific DNA Helicase Associated with the Maintenance of Genomic G/C Tracts
London, T. B. C., Barber, L. J., Mosedale, G., Kelly, G. P., Balasubramanian, S., Hickson, I. D., Boulton, S. J., & Hiom, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808152200 · Cited by 252
The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
Minsky, N., & Oren, M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.016 · Cited by 204
Nishikawa, H., Ooka, S., Sato, K., Arima, K., Okamoto, J., Klevit, R. E., Fukuda, M., & Ohta, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308540200 · Cited by 194
Targeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry?
Wade, M., & Wahl, G. M. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0423 · Cited by 170
Stabilization of the E3 Ubiquitin Ligase Nrdp1 by the Deubiquitinating Enzyme USP8
Wu, X., Yen, L., Irwin, L., Sweeney, C., & Carraway, K. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7748-7757.2004 · Cited by 144
BRCA1-independent ubiquitination of FANCD2
Vandenberg, C. J., Gergely, F., Ong, C. Y., Pace, P., Mallery, D. L., Hiom, K., & Patel, K. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00281-8 · Cited by 131
Self-citationThe role of BRCA1 in DNA double-strand repair: Past and present
Caestecker, K. W., & Van de Walle, G. R. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.11.013 · Cited by 108
Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme
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Atypical plant homeodomain of UBR7 functions as an H2BK120Ub ligase and breast tumor suppressor
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Wei, L., Lan, L., Yasui, A., Tanaka, K., Saijo, M., Matsuzawa, A., Kashiwagi, R., Maseki, E., Hu, Y., Parvin, J. D., et al. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.02037.x · Cited by 48
Stabilization of MCRS1 by BAP1 Prevents Chromosome Instability in Renal Cell Carcinoma
Peng, J., Ma, J., Li, W., Mo, R., Zhang, P., Gao, K., Jin, X., Xiao, J., Wang, C., & Fan, J. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.08.013 · Cited by 46
SIRT2 promotes BRCA1-BARD1 heterodimerization through deacetylation
Minten, E. V., Kapoor-Vazirani, P., Li, C., Zhang, H., Balakrishnan, K., & Yu, D. S. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108921 · Cited by 34
E3 ubiquitin ligases and their therapeutic potential in disease Management
Madhukar, G., Haque, M. A., Khan, S., Kim, J.-J., & Danishuddin (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116875 · Cited by 26
Metadata
- Authors
- Mallery, D. L.
- Venue
- The EMBO Journal
- Published
- 2002-12-16
- Volume
- 21
- Issue
- 24
- Pages
- 6755-6762
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2010369105
- Cited by
- 282
- References
- 5
- FWCI
- 4.86
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
