Literature summary for 3.4.21.98 extracted from

Wei, Y.; Yang, J.; Kishore Sakharkar, M.; Wang, X.; Liu, Q.; Du, J.; Zhang, J.J.
Evaluating the inhibitory effect of eight compounds from Daphne papyracea against the NS3/4A protease of hepatitis C virus (2018), Nat. Prod. Res., 0, 1-4 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
(+)-usnic acid	90.7% inhibition, the most active compound and could be used as a lead compound in developing novel anti-HCV agents. The major amino acid residues of NS3 protease likely involved in the interaction with (+)-usnic acid are Gln41, Ser42, Phe43, His57, Arg10	Hepacivirus C
1-4'-hydroxyphenyl-5-phenyl-2(E)-en-1-pentanone	56.5% inhibition	Hepacivirus C
3beta-O-acetyl-olean-12-en	29.0% inhibition	Hepacivirus C
boceprevir	-	Hepacivirus C
daphneolon	63.6% inhibition	Hepacivirus C
daphneticin	69.9% inhibition	Hepacivirus C
daphnetin	79.5% inhibition	Hepacivirus C
daphnoretin	36.5% inhibition	Hepacivirus C
embelin	-	Hepacivirus C
hydrangetin	72.5% inhibition	Hepacivirus C
additional information	the ethyl acetate extraction of Daphne papyracea exhibits an inhibitory effect towards the HCV NS3/4A protease. Eight compounds are identified from the extract. Molecular docking study of the identified inhibitory compounds against HCV NS3/4A protease using boceprevir as a positive control, docking scores, overview	Hepacivirus C

Organism

Organism	UniProt	Comment	Textmining
Hepacivirus C	-	-	-

Synonyms

Synonyms	Comment	Organism
NS3/4A protease	-	Hepacivirus C

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Hepacivirus C

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Release 2023.1 (January 2023)