The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Activity-Based Chemical Proteomics Accelerates Inhibitor Development for Deubiquitylating Enzymes
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Citations
Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 2×
“The increase in p53 protein induces a feedback mechanism that stimulates additional HDM2 (Vogelstein et al., 2000).”
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628
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-citationUbiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets
Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563 · cited 2×
“Successful drug development within the ubiquitin proteasome system (UPS) has enormous potential for the treatment of human disease, but faces considerable challenges (Bedford et al., 2011; Nalepa et al., 2006).”
The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network
Song, M. S., Salmena, L., Carracedo, A., Egia, A., Lo-Coco, F., Teruya-Feldstein, J., & Pandolfi, P. P. (2008) · Nature · doi:10.1038/nature07290 · Cited by 548
Disruption 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
Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260
Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226
Self-citationOvaa, H., Kessler, B. M., Rolén, U., Galardy, P. J., Ploegh, H. L., & Masucci, M. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308411100 · Cited by 190
Self-citation
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
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
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
Self-citationDeubiquitylases 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
p53 modifications: exquisite decorations of the powerful guardian
Liu, Y., Tavana, O., & Gu, W. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz060 · Cited by 392
Metadata
- Authors
- Altun, M., Kramer, H. B., Willems, L. I., McDermott, J. L., Leach, C. A., Goldenberg, S. J., Kumar, K. G. S., Konietzny, R., Fischer, R., Kogan, E., Mackeen, M. M., McGouran, J., Khoronenkova, S. V., Parsons, J. L., Dianov, G. L., Nicholson, B., & Kessler, B. M.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 18
- Issue
- 11
- Pages
- 1401-1412
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W2072310367
- Cited by
- 402
- References
- 11
- FWCI
- 8.46
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Activity-Based Chemical Proteomics Accelerates Inhibitor Development for Deubiquitylating Enzymes. https://app.cochat.ai/papers/10.1016/j.chembiol.2011.08.018
- The paper
- Altun, M., Kramer, H. B., Willems, L. I., McDermott, J. L., Leach, C. A., Goldenberg, S. J., Kumar, K. G. S., Konietzny, R., Fischer, R., Kogan, E., Mackeen, M. M., McGouran, J., Khoronenkova, S. V., Parsons, J. L., Dianov, G. L., Nicholson, B., & Kessler, B. M. (2011). Activity-Based Chemical Proteomics Accelerates Inhibitor Development for Deubiquitylating Enzymes. Chemistry & Biology. https://doi.org/10.1016/j.chembiol.2011.08.018
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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.
