1374334-32-3Relevant academic research and scientific papers
Structure-Based Drug Design of Bisubstrate Inhibitors of Phenylethanolamine N-Methyltransferase Possessing Low Nanomolar Affinity at Both Substrate Binding Domains1
Lu, Jian,Bart, Aaron G.,Wu, Qian,Criscione, Kevin R.,McLeish, Michael J.,Scott, Emily E.,Grunewald, Gary L.
, p. 13878 - 13898 (2020)
The enzyme phenylethanolamine N-methyltransferase (PNMT, EC 2.1.1.28) catalyzes the final step in the biosynthesis of epinephrine and is a potential drug target, primarily for the control of hypertension. Unfortunately, many potent PNMT inhibitors also po
BORONATES AS ARGINASE INHIBITORS
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Page/Page column 83-84, (2012/05/19)
Compounds according to Formula I are potent inhibitors of Arginase I and II activity: (I) where R1, R2, R3, R4, D, W, X, Y, and Z are defined in the specification. The invention also provides pharmaceutical compositions of the compounds and methods of their use in treating or preventing a disease or a condition associated with arginase activity.
