Cinanserin Is an Inhibitor of the 3C-Like Proteinase of Severe Acute Respiratory Syndrome Coronavirus and Strongly Reduces Virus Replication In Vitro

@article{Chen2005CinanserinIA,
  title={Cinanserin Is an Inhibitor of the 3C-Like Proteinase of Severe Acute Respiratory Syndrome Coronavirus and Strongly Reduces Virus Replication In Vitro},
  author={Li-li Chen and Chunshan Gui and Xiaomin Luo and Qingang Yang and Stephan G{\"u}nther and Elke Scandella and Christian Drosten and Dong-lu Bai and X C He and Burkhard Ludewig and Jing Chen and Haibin Luo and Yiming Yang and Yifu Yang and Jianping Zou and Volker Thiel and Kaixian Chen and Jianhua Shen and Xu Shen and Hualiang Jiang},
  journal={Journal of Virology},
  year={2005},
  volume={79},
  pages={7095 - 7103}
}
ABSTRACT The 3C-like proteinase (3CLpro) of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is one of the most promising targets for anti-SARS-CoV drugs due to its crucial role in the viral life cycle. In this study, a database containing structural information of more than 8,000 existing drugs was virtually screened by a docking approach to identify potential binding molecules of SARS-CoV 3CLpro. As a target for screening, both a homology model and the crystallographic… 
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A programme of structure-assisted drug design and high-throughput screening identifies six compounds that inhibit the main protease of SARS-CoV-2, demonstrating the ability of this strategy to isolate drug leads with clinical potential.
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TLDR
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Design and Evaluation of Anti-SARS-Coronavirus Agents Based on Molecular Interactions with the Viral Protease
TLDR
A series of studies on SARS-CoV are reviewed, focusing on the development of inhibitors for the SARS -CoV 3CLpro based on molecular interactions with the 3CL protease, which is thought to be an ideal therapeutic agent against SARS, MERS, or COVID-19.
Characterization and Inhibition of the Main Protease of Severe Acute Respiratory Syndrome Coronavirus
TLDR
Current developments in anti‐SARS agents targeting 3CLpro and the application of the mutant protease as a tag‐cleavage endopeptidase are summarized.
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TLDR
A search for analogues with common substructure in the Maybridge, ChemBridge, and SPECS_SC databases led to the identification of another 25 compounds that exhibited inhibition against SARS-CoV 3CL(pro) (IC(50) = 3-1,000 microM).
Substrate specificity profiling and identification of a new class of inhibitor for the major protease of the SARS coronavirus.
TLDR
A complete description of the tetrapeptide substrate specificity of 3Clpro is reported using fully degenerate peptide libraries consisting of all 160,000 possible naturally occurring tetrapptides to provide the foundation for a rational small-molecule inhibitor design effort based upon the inhibitor scaffold identified, the crystal structure of the complex, and a more complete understanding of P1-P4 substrate specificity.
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