Literature summary for 3.4.22.28 extracted from

Steindl, T.; Laggner, C.; Langer, T.
Human rhinovirus 3C protease: generation of pharmacophore models for peptidic and nonpeptidic inhibitors and their application in virtual screening (2005), J. Chem. Inf. Model., 45, 716-724.

Search for more literature for 3.4.22.28

Application

Application	Comment	Organism
drug development	three-dimensional pharmacophore models for peptidic and small organic nonpeptidic inhibitors of the human rhinovirus 3C protease, structure-based and ligand-based approach, using the software package Catalyst	Human rhinovirus sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	inhibitors possess an electophilic moiety, often a Michael acceptor function, which covalently binds to a cysteine in the active site of the enzyme, key step for virus inactivation	Human rhinovirus sp.

Organism

Organism	UniProt	Comment	Textmining
Human rhinovirus sp.	-	-	-

Synonyms

Synonyms	Comment	Organism
3C protease	-	Human rhinovirus sp.

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Release 2023.1 (January 2023)