The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design
Open accessAbstract
This review focuses on the important contributions that macromolecular crystallography has made over the past 12 years to elucidating structures and mechanisms of the essential proteases of coronaviruses, the main protease (M pro) and the papain‐like protease (PL pro). The role of X‐ray crystallography in structure‐assisted drug discovery against these targets is discussed. Aspects dealt with in this review include the emergence of the SARS coronavirus in 2002–2003 and of the MERS coronavirus 10 years later and the origins of these viruses. The crystal structure of the free SARS coronavirus M pro and its dependence on pH is discussed, as are efforts to design inhibitors on the basis of these structures. The mechanism of maturation of the enzyme from the viral polyprotein is still a matter of debate. The crystal structure of the SARS coronavirus PL pro and its complex with ubiquitin is also discussed, as is its orthologue from MERS coronavirus. Efforts at predictive structure‐based inhibitor development for bat coronavirus M pro s to increase the preparedness against zoonotic transmission to man are described as well. The paper closes with a brief discussion of structure‐based discovery of antivirals in an academic setting.
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Cites
Identification of a novel coronavirus in patients with severe acute respiratory syndrome
Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
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Cited by
SARS and MERS: recent insights into emerging coronaviruses
de Wit, E., van Doremalen, N., Falzarano, D., & Munster, V. J. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.81 · Cited by 3,510
Zhang, L., Lin, D., Sun, X., Curth, U., Drosten, C., Sauerhering, L., Becker, S., Rox, K., & Hilgenfeld, R. (2020) · Science · doi:10.1126/science.abb3405 · Cited by 2,895
Self-citationOral Nirmatrelvir for High-Risk, Nonhospitalized Adults with Covid-19
Hammond, J., Leister-Tebbe, H., Gardner, A., Abreu, P., Bao, W., Wisemandle, W., Baniecki, M., Hendrick, V. M., Damle, B., Simón-Campos, A., et al. (2022) · New England Journal of Medicine · doi:10.1056/nejmoa2118542 · Cited by 2,323
Kneller, D. W., Phillips, G., O’Neill, H. M., Jedrzejczak, R., Stols, L., Langan, P., Joachimiak, A., Coates, L., & Kovalevsky, A. (2020) · Nature Communications · doi:10.1038/s41467-020-16954-7 · Cited by 474
Rut, 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
Metadata
- Authors
- Hilgenfeld, R.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2014-08-11
- Volume
- 281
- Issue
- 18
- Pages
- 4085-4096
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2163761019
- Cited by
- 660
- References
- 3
- FWCI
- 5.84
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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