EC Number   |
Application |
Reference |
|---|
   3.4.22.69 | analysis |
developing a novel red-shifted fluorescence-based assay for 3CLpro and its application for identifying small-molecule anti-SARS agents from marine organisms |
678512 |
| 3.4.22.69 | analysis |
development of a dual-color probe for the simultaneous detection of Mpro and PLpro by FRET in vitro and in cells. The probe produces fluorescence from both the Cy3 and Cy5 fluorophores that are cleaved by Mpro and PLpro |
763894 |
| 3.4.22.69 | analysis |
FRET-based method to assess the proteolytic activity of SARS-CoV-2 3CLpro using intramolecularly quenched fluorogenic peptide substrates corresponding to the cleavage sequence of SARS-CoV-2 3CLpro |
764084 |
| 3.4.22.69 | analysis |
quantitative structure-activity relationship model, molecular docking studies and molecular dynamics simulation to identify inhibitors, the model is applied to three large databases and reports top 25 compounds from each database |
765106 |
| 3.4.22.69 | analysis |
SARS-CoV-2-infected Vero E6 cell viability assay for detection of antiviral activity |
765227 |
| 3.4.22.69 | drug development |
coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus infections, including severe acute respiratory syndrome (SARS) |
731320 |
| 3.4.22.69 | drug development |
the enzyme is an attractive target for the development of anti-SARS drugs |
731060 |
| 3.4.22.69 | medicine |
patients infected with a SARS-Cov-2 sub-lineage (B.1.1.284) carrying the Pro108Ser mutation in 3CLpro tend to have a comparatively milder clinical course than patients infected with the same sub-lineage of virus not carrying the mutation |
765793 |
| 3.4.22.69 | medicine |
SARS-3CLpro is a viral cysteine protease critical to the life cycle of the pathogen and hence a therapeutic target of importance |
691218 |
| 3.4.22.69 | medicine |
this enzyme is a target for the design of potential anti-SARS drugs |
691200 |
