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The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition.
Sacco, Michael Dominic; Hu, Yanmei; Gongora, Maura Verenice; Meilleur, Flora; Kemp, Michael Trent; Zhang, Xiujun; Wang, Jun; Chen, Yu.
Affiliation
  • Sacco MD; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
  • Hu Y; Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, the State University of New Jersey, Piscataway, NJ, USA.
  • Gongora MV; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
  • Meilleur F; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC, USA.
  • Kemp MT; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, USA.
  • Zhang X; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
  • Wang J; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
  • Chen Y; Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, the State University of New Jersey, Piscataway, NJ, USA. junwang@pharmacy.rutgers.edu.
Cell Res ; 32(5): 498-500, 2022 05.
Article in En | MEDLINE | ID: mdl-35292745
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Cell Res Year: 2022 Type: Article Affiliation country: United States
Fulltext
Print
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PubMed Links
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Cell Res Year: 2022 Type: Article Affiliation country: United States