| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T141 |
0-123 |
Sentence |
denotes |
N-(benzo[1,2,3]triazol-1-yl)-N-(benzyl) acetamido) phenyl) carboxamides are also found to be important inhibitors of CLPro. |
| T142 |
124-202 |
Sentence |
denotes |
The structure of CLPro inhibitor is with ML188 (IC50 1.5 μM) is reported (CID: |
| T143 |
203-220 |
Sentence |
denotes |
46897844, PDB ID: |
| T144 |
221-287 |
Sentence |
denotes |
3V3M).[7980] Another structure with CLPro inhibitor ML300 (PDB ID: |
| T145 |
288-299 |
Sentence |
denotes |
4MDS, IC50: |
| T146 |
300-807 |
Sentence |
denotes |
6.2 μM) is reported.[79] Some metal-conjugated and peptidomimetic compounds showed inhibitory activity against 3CLpro.[77] Some of the small molecules also act as an inhibitor that is arylboronic acids, quinolinecarboxylate derivatives, thiophenecarboxylate, and phthalhydrazide-substituted ketoglutamine analogs.[77] Some flavonoids are also reported to inhibit Mpro.[75] GC376 also has protease inhibitor activity.[81] A crystal structure of Mpro with small molecule inhibitor N3 is also reported (PDB ID: |
| T147 |
808-1164 |
Sentence |
denotes |
2AMQ).[82] Lopinavir and ritonavir, which are the inhibitors of HIV protease, also inhibit Mpro.[83] In silico studies directed that among commercially available drugs, colistin, valrubicin, icatibant, bepotastine, epirubicin, epoprostenol, vapreotide, aprepitant, caspofungin, and perphenazine also bind to the lopinavir/ritonavir-binding site on CoV.[83] |
