The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases
Open accessAbstract
Active-site directed probes are powerful in studies of enzymatic function. We report an active-site directed probe based on a warhead so far considered unreactive. By replacing the C-terminal carboxylate of ubiquitin (Ub) with an alkyne functionality, a selective reaction with the active-site cysteine residue of de-ubiquitinating enzymes was observed. The resulting product was shown to be a quaternary vinyl thioether, as determined by X-ray crystallography. Proteomic analysis of proteins bound to an immobilized Ub alkyne probe confirmed the selectivity toward de-ubiquitinating enzymes. The observed reactivity is not just restricted to propargylated Ub, as highlighted by the selective reaction between caspase-1 (interleukin converting enzyme) and a propargylated peptide derived from IL-1β, a caspase-1 substrate.
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Tornøe, C. W., Christensen, C., & Meldal, M. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo011148j · Cited by 8,696
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Self-citationChemistry-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 by
Mevissen, T. E. T., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., El Oualid, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.046 · Cited by 626
Self-citationRut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S. J., El Oualid, F., Huang, T. T., Bekes, M., Drag, M., et al. (2020) · Science Advances · doi:10.1126/sciadv.abd4596 · Cited by 459
Abdul Rehman, S. A., Kristariyanto, Y. A., Choi, S.-Y., Nkosi, P. J., Weidlich, S., Labib, K., Hofmann, K., & Kulathu, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.009 · Cited by 363
Self-citationRapid Covalent-Probe Discovery by Electrophile-Fragment Screening
Resnick, E., Bradley, A., Gan, J., Douangamath, A., Krojer, T., Sethi, R., Geurink, P. P., Aimon, A., Amitai, G., Bellini, D., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b02822 · Cited by 335
Self-citationActivity-Based Profiling of Proteases
Sanman, L. E., & Bogyo, M. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035352 · Cited by 330
Metadata
- Authors
- Ekkebus, R., van Kasteren, S. I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P. P., de Jong, A., Goerdayal, S., Neefjes, J., Heck, A. J. R., Komander, D., & Ovaa, H.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-02-15
- Volume
- 135
- Issue
- 8
- Pages
- 2867-2870
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2099598643
- Cited by
- 347
- References
- 4
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ekkebus, R., van Kasteren, S. I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P. P., de Jong, A., Goerdayal, S., Neefjes, J., Heck, A. J. R., Komander, D., & Ovaa, H. (2013). On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases. Journal of the American Chemical Society. https://doi.org/10.1021/ja309802n
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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.
