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10.1146/annurev-pharmtox-061220-093932

http://scihub22266oqcxt.onion/10.1146/annurev-pharmtox-061220-093932
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32574109!ä!32574109

suck abstract from ncbi


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pmid32574109      Annu+Rev+Pharmacol+Toxicol 2021 ; 61 (ä): 465-493
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  • Structural Basis of SARS-CoV-2- and SARS-CoV-Receptor Binding and Small-Molecule Blockers as Potential Therapeutics #MMPMID32574109
  • Sivaraman H; Er SY; Choong YK; Gavor E; Sivaraman J
  • Annu Rev Pharmacol Toxicol 2021[Jan]; 61 (ä): 465-493 PMID32574109show ga
  • Over the past two decades, deadly coronaviruses, with the most recent being the severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) 2019 pandemic, have majorly challenged public health. The path for virus invasion into humans and other hosts is mediated by host-pathogen interactions, specifically virus-receptor binding. An in-depth understanding of the virus-receptor binding mechanism is a prerequisite for the discovery of vaccines, antibodies, and small-molecule inhibitors that can interrupt this interaction and prevent or cure infection. In this review, we discuss the viral entry mechanism, the known structural aspects of virus-receptor interactions (SARS-CoV-2 S/humanACE2, SARS-CoV S/humanACE2, and MERS-CoV S/humanDPP4), the key protein domains and amino acid residues involved in binding, and the small-molecule inhibitors and other drugs that have (as of June 2020) exhibited therapeutic potential. Specifically, we review the potential clinical utility of two transmembrane serine protease 2 (TMPRSS2)-targeting protease inhibitors, nafamostat mesylate and camostat mesylate, as well as two novel potent fusion inhibitors and the repurposed Ebola drug, remdesivir, which is specific to RNA-dependent RNA polymerase, against human coronaviruses, including SARS-CoV-2.
  • |*COVID-19 Drug Treatment[MESH]
  • |*Small Molecule Libraries[MESH]
  • |Angiotensin-Converting Enzyme 2/*drug effects[MESH]
  • |Antiviral Agents/*pharmacology/*therapeutic use[MESH]
  • |Humans[MESH]
  • |Protease Inhibitors/therapeutic use[MESH]


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