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Science, ISSN 0036-8075, 6/2003, Volume 300, Issue 5626, pp. 1763 - 1767
A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (M , also called ), which... 
Enzymes | Molecules | Coronavirus | Atoms | SARS | Reports | Dimers | Polyproteins | SARS virus | Monomers | Crystal structure | VIRUS-ENCODED PROTEINASES | 229E 3C-LIKE PROTEINASE | MULTIDISCIPLINARY SCIENCES | PROTEASES | Cysteine Endopeptidases - chemistry | Coronavirus 229E, Human - enzymology | Humans | Cysteine Proteinase Inhibitors - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Cysteine Endopeptidases - metabolism | Pyrrolidinones - metabolism | Pyrrolidinones - pharmacology | Drug Design | Amino Acid Chloromethyl Ketones - metabolism | Cysteine Proteinase Inhibitors - chemistry | Binding Sites | Dimerization | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Transmissible gastroenteritis virus - enzymology | Catalytic Domain | Protein Structure, Secondary | Amino Acid Chloromethyl Ketones - chemistry | Isoxazoles - metabolism | Crystallization | Models, Molecular | Recombinant Proteins - chemistry | SARS Virus - drug effects | Antiviral Agents | Isoxazoles - chemistry | Severe Acute Respiratory Syndrome - drug therapy | Pyrrolidinones - chemistry | Isoxazoles - pharmacology | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation | SARS Virus - enzymology | Severe acute respiratory syndrome | Research | Coronaviruses | Proteins | Viruses | Drug therapy | Index Medicus
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