The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Mechanism of USP7/HAUSP Activation by Its C-Terminal Ubiquitin-like Domain and Allosteric Regulation by GMP-Synthetase
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Citations
Cites
Coot : model-building tools for molecular graphics
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
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“The deubiquitinating enzyme (DUB) ubiquitin-specific protease 7 (USP7), also known as herpes virus-associated ubiquitin-specific protease (HAUSP), regulates the function of the tumor suppressor p53 that is mutated or inactivated in 50% of human cancers (Vogelstein et al., 2000).”
BackgroundUbiquitination regulates PTEN nuclear import and tumor suppression
Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748
A dynamic role of HAUSP in the p53-Mdm2 pathway
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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
Self-citationDisruption of HAUSP gene stabilizes p53.
Cummins, J. M., Rago, C., Kohli, M., Kinzler, K. W., Lengauer, C., & Vogelstein, B. (2004) · Nature · doi:10.1038/nature02501 · Cited by 379
HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53
Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361
Molecular recognition of p53 and MDM2 by USP7/HAUSP.
Sheng, Y., Saridakis, V., Sarkari, F., Duan, S., Wu, T., Arrowsmith, C. H., & Frappier, L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1067 · Cited by 315
Monoubiquitylation promotes mitochondrial p53 translocation
Marchenko, N. D., Wolff, S., Erster, S., Becker, K., & Moll, U. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601560 · Cited by 286
Cited by
Deubiquitylating enzymes and drug discovery: emerging opportunities
Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940
Molecular basis of USP7 inhibition by selective small-molecule inhibitors.
Turnbull, A. P., Ioannidis, S., Krajewski, W. W., Pinto-Fernandez, A., Heride, C., Martin, A. C. L., Tonkin, L. M., Townsend, E. C., Buker, S. M., Lancia, D. R., et al. (2017) · Nature · doi:10.1038/nature24451 · Cited by 463
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 425
Discovery of specific inhibitors of human USP7/HAUSP deubiquitinating enzyme.
Reverdy, C., Conrath, S., Lopez, R., Planquette, C., Atmanene, C., Collura, V., Harpon, J., Battaglia, V., Vivat, V., Sippl, W., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.02.007 · Cited by 270
Hao, Y.-H., Fountain, M. D., Fon Tacer, K., Xia, F., Bi, W., Kang, S.-H. L., Patel, A., Rosenfeld, J. A., Le Caignec, C., Isidor, B., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.033 · Cited by 206
Metadata
- Authors
- Faesen, A. C., Dirac, A. M. G., Shanmugham, A., Ovaa, H., Perrakis, A., & Sixma, T. K.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 44
- Issue
- 1
- Pages
- 147-159
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2037239543
- Cited by
- 248
- References
- 16
- FWCI
- 5.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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- The paper
- Faesen, A. C., Dirac, A. M. G., Shanmugham, A., Ovaa, H., Perrakis, A., & Sixma, T. K. (2011). Mechanism of USP7/HAUSP Activation by Its C-Terminal Ubiquitin-like Domain and Allosteric Regulation by GMP-Synthetase. Molecular Cell. https://doi.org/10.1016/j.molcel.2011.06.034
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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.