Selected article for: "acid viral and acute respiratory syndrome"
Author: Ghosh, Arun K.; Xi, Kai; Johnson, Michael E.; Baker, Susan C.; Mesecar, Andrew D.
Title: Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy
  • Cord-id: 1wae0134
  • Document date: 2006_12_31
    • ID: 1wae0134
    Snippet: Publisher Summary Proteolytic processing of the coronavirus replicase polyproteins is essential for ongoing viral ribonucleic acid (RNA) synthesis. Therefore, the severe acute respiratory syndrome (SARS)-coronaviruses (SARS-CoV) proteases are attractive targets for the development of antiviral drugs to reduce viral replication and pathogenicity. The structure and activity of the coronavirus 3C-like protease (3CLpro) has already been elucidated, and the design of inhibitors to 3CLpro as therapeut
    Document: Publisher Summary Proteolytic processing of the coronavirus replicase polyproteins is essential for ongoing viral ribonucleic acid (RNA) synthesis. Therefore, the severe acute respiratory syndrome (SARS)-coronaviruses (SARS-CoV) proteases are attractive targets for the development of antiviral drugs to reduce viral replication and pathogenicity. The structure and activity of the coronavirus 3C-like protease (3CLpro) has already been elucidated, and the design of inhibitors to 3CLpro as therapeutics has been proposed. The chapter discusses SARS-CoV 3CLpro inhibitors that include covalent inhibitors, noncovalent inhibitors, and inhibitors from screening. SARS-CoV papain-like protease (PLpro) is considered an equally viable target to 3CLpro for drug design because both are essential for viral replication. However, PLpro has likely not been pursued because of the paucity of structural information. Several compounds have been identified that have shown inhibitory activity against SARS-CoV. However, no information regarding their mechanism of action or the corresponding target is known. Glycyrrhizin showed inhibitory activity for SARS-CoV replication with EC50 = 300 mg/L after virus absorption in Vero cells. Some glycyrrhizin acid derivatives were found to inhibit SARS-CoV replication in vitro with EC50 values ranging from 5 to 50 μM. Unfortunately, these compounds show high cytotoxity.

    Search related documents:
    Co phrase search for related documents
    • acid amide and active site: 1, 2, 3
    • acid amide and activity structure: 1
    • acid amide and acute respiratory syndrome: 1
    • acid derivative and action mechanism: 1, 2, 3, 4, 5
    • acid derivative and active site: 1, 2
    • acid derivative and acute respiratory syndrome: 1, 2
    • acid derivative and low molecular: 1
    • acidic environment and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7
    • action mechanism and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25
    • action mechanism and low micromolar range: 1, 2, 3, 4, 5
    • action mechanism and low molecular: 1, 2, 3, 4
    • active pocket and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11
    • active site and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25
    • active site and additional product: 1
    • active site and low micromolar range: 1, 2, 3, 4, 5, 6
    • active site and low micromolar range inhibition constant: 1
    • active site and low molecular: 1, 2, 3, 4, 5, 6, 7, 8
    • active site catalytic dyad and low micromolar range inhibition constant: 1
    • active site catalytic dyad and low molecular: 1