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10.1021/acs.jmedchem.0c01140

http://scihub22266oqcxt.onion/10.1021/acs.jmedchem.0c01140
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33186044!7688049!33186044
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suck abstract from ncbi


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pmid33186044      J+Med+Chem 2022 ; 65 (4): 2716-2746
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  • Targeting SARS-CoV-2 Proteases and Polymerase for COVID-19 Treatment: State of the Art and Future Opportunities #MMPMID33186044
  • Cannalire R; Cerchia C; Beccari AR; Di Leva FS; Summa V
  • J Med Chem 2022[Feb]; 65 (4): 2716-2746 PMID33186044show ga
  • The newly emerged coronavirus, called SARS-CoV-2, is the causing pathogen of pandemic COVID-19. The identification of drugs to treat COVID-19 and other coronavirus diseases is an urgent global need, thus different strategies targeting either virus or host cell are still under investigation. Direct-acting agents, targeting protease and polymerase functionalities, represent a milestone in antiviral therapy. The 3C-like (or Main) protease (3CL(pro)) and the nsp12 RNA-dependent RNA-polymerase (RdRp) are the best characterized SARS-CoV-2 targets and show the highest degree of conservation across coronaviruses fostering the identification of broad-spectrum inhibitors. Coronaviruses also possess a papain-like protease, another essential enzyme, still poorly characterized and not equally conserved, limiting the identification of broad-spectrum agents. Herein, we provide an exhaustive comparative analysis of SARS-CoV-2 proteases and RdRp with respect to other coronavirus homologues. Moreover, we highlight the most promising inhibitors of these proteins reported so far, including the possible strategies for their further development.
  • |*COVID-19 Drug Treatment[MESH]
  • |Antiviral Agents/chemistry/*pharmacology[MESH]
  • |COVID-19/metabolism[MESH]
  • |Coronavirus 3C Proteases/*antagonists & inhibitors/metabolism[MESH]
  • |Humans[MESH]
  • |Molecular Structure[MESH]
  • |Protease Inhibitors/chemistry/*pharmacology[MESH]
  • |RNA-Dependent RNA Polymerase/*antagonists & inhibitors/metabolism[MESH]


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