Literature summary for 3.4.22.28 extracted from

Binford, S.L.; Maldonado, F.; Brothers, M.A.; Weady, P.T.; Zalman, L.S.; Meador, J.W.; Matthews, D.A.; Patick, A.K.
Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor (2005), Antimicrob. Agents Chemother., 49, 619-626.

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Application

Application	Comment	Organism
medicine	conservation of critical amino acid residues in 3C protease and the potent, broad-spectrum activity of rupintrivir highlight the advantage of 3C protease as an antiviral target	enterovirus
medicine	conservation of critical amino acid residues in 3C protease and the potent, broad-spectrum activity of rupintrivir highlight the advantage of 3C protease as an antiviral target	Human rhinovirus sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
rupintrivir	irreversible inhibitor of human enterovirus strains (4 of 4)	enterovirus
rupintrivir	potent in vitro activity against 23 clinical isolates tested in H1-HeLa cell protection assays	Human rhinovirus sp.

Organism

Organism	UniProt	Comment	Textmining
enterovirus	-	and strains CVB5, EV6, and EV9	-
enterovirus CVB2	-	and strains CVB5, EV6, and EV9	-
Human rhinovirus sp.	-	23 clinical isolates	-

Synonyms

Synonyms	Comment	Organism
3C protease	-	enterovirus
3C protease	-	Human rhinovirus sp.

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Release 2023.1 (January 2023)