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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS Drugs

Anand, Kanchan, Ziebuhr, John, Wadhwani, Parvesh, Mesters, Jeroen R., Hilgenfeld, Rolf·2003·Science

Abstract

A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (M pro , also called 3CL pro ), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) M pro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] M pro , and we constructed a homology model for SARS coronavirus (SARS-CoV) M pro . The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV M pro -mediated cleavage of a TGEV M pro substrate. Molecular modeling suggests that available rhinovirus 3C pro inhibitors may be modified to make them useful for treating SARS.

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Metadata

Authors
Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J. R., & Hilgenfeld, R.
Venue
Science
Published
2003-06-13
Volume
300
Issue
5626
Pages
1763-1767
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2027484375
Cited by
1,728
References
1
FWCI
52.80
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS Drugs. https://app.cochat.ai/papers/10.1126/science.1085658
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Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J. R., & Hilgenfeld, R. (2003). Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS Drugs. Science. https://doi.org/10.1126/science.1085658

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.