S-Nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease

Bioorganic & Medicinal Chemistry Letters
2000.0

Abstract

Human rhinovirus (HRV) 3C protease was inactivated by a series of S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (kinact/K(I)) ranging from 131 to 5360 M(-1) min(-1). The inactive enzyme could be re-activated by DTT, GSH and ascorbate, which indicated the inactivation mechanism was through an S-transnitrosylation process.

DOI： 10.1016/s0960-894x(00)00420-0

Knowledge Graph

Similar Paper

S-Nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease
Bioorganic & Medicinal Chemistry Letters 2000.0
Design and synthesis of irreversible depsipeptidyl human rhinovirus 3C protease inhibitors
Bioorganic & Medicinal Chemistry Letters 2001.0
Small peptidic aldehyde inhibitors of human rhinovirus 3C protease
Bioorganic & Medicinal Chemistry Letters 1996.0
S-nitrosation of proteins by N-methyl-N-nitrosoanilines
Bioorganic & Medicinal Chemistry Letters 1996.0
Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 4. Incorporation of P<sub>1</sub> Lactam Moieties as <scp>l</scp>-Glutamine Replacements
Journal of Medicinal Chemistry 1999.0
New anti-viral drugs for the treatment of the common cold
Bioorganic &amp; Medicinal Chemistry 2008.0
Dipeptidyl Nitroalkenes as Potent Reversible Inhibitors of Cysteine Proteases Rhodesain and Cruzain
ACS Medicinal Chemistry Letters 2016.0
Non-covalent inhibitors of rhinovirus 3C protease
Bioorganic &amp; Medicinal Chemistry Letters 2011.0
Design and structure–activity relationships of novel inhibitors of human rhinovirus 3C protease
Bioorganic &amp; Medicinal Chemistry Letters 2016.0
Substituted Benzamide Inhibitors of Human Rhinovirus 3C Protease:  Structure-Based Design, Synthesis, and Biological Evaluation
Journal of Medicinal Chemistry 2000.0