The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
Open accessAbstract
A large-scale screen to target SARS-CoV-2: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome is initially expressed as two large polyproteins. Its main protease, M pro , is essential to yield functional viral proteins, making it a key drug target. Günther et al. used x-ray crystallography to screen more than 5000 compounds that are either approved drugs or drugs in clinical trials. The screen identified 37 compounds that bind to M pro . High-resolution structures showed that most compounds bind at the active site but also revealed two allosteric sites where binding of a drug causes conformational changes that affect the active site. In cell-based assays, seven compounds had antiviral activity without toxicity. The most potent, calpeptin, binds covalently in the active site, whereas the second most potent, pelitinib, binds at an allosteric site. Science , this issue p. 642
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Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Drug repurposing: progress, challenges and recommendations
Pushpakom, S., Iorio, F., Eyers, P. A., Escott, K. J., Hopper, S., Wells, A., Doig, A., Guilliams, T., Latimer, J., McNamee, C., et al. (2019) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.168 · Cited by 4,718
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Fadini, A., Li, M., McCoy, A. J., Banjara, S., Okumura, H., Napier, E., Fontana, P., Khan, A. R., Jovine, L., Terwilliger, T. C., et al. (2026) · Nature Methods · doi:10.1038/s41592-026-03047-4 · Cited by 22
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Metadata
- Authors
- Günther, S., Reinke, P. Y. A., Fernández-García, Y., Lieske, J., Lane, T. J., Ginn, H. M., Koua, F. H. M., Ehrt, C., Ewert, W., Oberthuer, D., Yefanov, O., Meier, S., Lorenzen, K., Krichel, B., Kopicki, J.-D., Gelisio, L., Brehm, W., Dunkel, I., Seychell, B., Gieseler, H., Norton-Baker, B., Escudero-Pérez, B., Domaracky, M., Saouane, S., Tolstikova, A., White, T. A., Hänle, A., Groessler, M., Fleckenstein, H., Trost, F., Galchenkova, M., Gevorkov, Y., Li, C., Awel, S., Peck, A., Barthelmess, M., Schlünzen, F., Lourdu Xavier, P., Werner, N., Andaleeb, H., Ullah, N., Falke, S., Srinivasan, V., França, B. A., Schwinzer, M., Brognaro, H., Rogers, C., Melo, D., Zaitseva-Doyle, J. J., Knoska, J., Peña-Murillo, G. E., Mashhour, A. R., Hennicke, V., Fischer, P., Hakanpää, J., Meyer, J., Gribbon, P., Ellinger, B., Kuzikov, M., Wolf, M., Beccari, A. R., Bourenkov, G., von Stetten, D., Pompidor, G., Bento, I., Panneerselvam, S., Karpics, I., Schneider, T. R., Garcia-Alai, M. M., Niebling, S., Günther, C., Schmidt, C., Schubert, R., Han, H., Boger, J., Monteiro, D. C. F., Zhang, L., Sun, X., Pletzer-Zelgert, J., Wollenhaupt, J., Feiler, C. G., Weiss, M. S., Schulz, E.-C., Mehrabi, P., Karničar, K., Usenik, A., Loboda, J., Tidow, H., Chari, A., Hilgenfeld, R., Uetrecht, C., Cox, R., Zaliani, A., Beck, T., Rarey, M., Günther, S., Turk, D., Hinrichs, W., Chapman, H. N., Pearson, A. R., Betzel, C., & Meents, A.
- Venue
- Science
- Published
- 2021-05-07
- Volume
- 372
- Issue
- 6542
- Pages
- 642-646
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3148554359
- Cited by
- 372
- References
- 2
- FWCI
- 22.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
