Abstract
A series of quinoxalinylurea-based inhibitors are synthesized and shown to be the novel and potent inhibitors against Jnk Stimulatory Phosphatase-1 (JSP-1), which is a special member of dual-specificity protein phosphatase (DSP) family. Biological assay and computational modeling studies showed the compounds were reversible and noncompetitive inhibitors of JSP-1. JSP-1 inhibitors may be useful for the treatment of inflammatory, vascular, neurodegenerative, metabolic, and oncological diseases in humans associated with dysfunctional Jnk signaling.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Allosteric Site
-
Dual-Specificity Phosphatases
-
Enzyme Inhibitors / chemical synthesis
-
Enzyme Inhibitors / pharmacology
-
Inhibitory Concentration 50
-
Mitogen-Activated Protein Kinase Phosphatases
-
Phosphoprotein Phosphatases / antagonists & inhibitors*
-
Protein Phosphatase 1
-
Protein Tyrosine Phosphatases / antagonists & inhibitors*
-
Quinoxalines / chemical synthesis*
-
Quinoxalines / pharmacology
-
Structure-Activity Relationship
-
Urea / chemical synthesis*
-
Urea / pharmacology
Substances
-
Enzyme Inhibitors
-
Quinoxalines
-
Urea
-
Mitogen-Activated Protein Kinase Phosphatases
-
Phosphoprotein Phosphatases
-
Protein Phosphatase 1
-
DUSP22 protein, human
-
Dual-Specificity Phosphatases
-
Protein Tyrosine Phosphatases