Cleavage at the nsp5/nsp6 site of SARS-CoV-2 main protease intermediate precursor is faster from a monomer than a dimer formSARS-CoV-2主蛋白酶中间前体在nsp5/nsp6位点的裂解，单体形式比二聚体形式更快。Journal of Biological ChemistryIF3.92026-03-200OAAI
Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent InhibitorsJOURNAL OF MEDICINAL CHEMISTRYIF6.82024-10-070PRE
Characterization of alternate encounter assemblies of SARS-CoV-2 main proteaseJOURNAL OF BIOLOGICAL CHEMISTRYIF3.92024-09-011OAAI
Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursorsCOMMUNICATIONS BIOLOGYIF5.12023-11-1311OAAI
Contribution of the catalytic dyad of SARS-CoV-2 main protease to binding covalent and noncovalent inhibitorsJOURNAL OF BIOLOGICAL CHEMISTRYIF3.92023-07-0114OAAI
Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domainCOMMUNICATIONS BIOLOGYIF5.12022-09-1619OAAI
Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitorCOMMUNICATIONS BIOLOGYIF5.12022-03-0133OAAI
Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitorsPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICAIF9.12011-05-1664OAAI
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