Discovery of LYS006, a Potent and Highly Selective Inhibitor of Leukotriene A4 Hydrolase
Author:
Funder
Novartis Institutes for BioMedical Research Inc.
Publisher
American Chemical Society (ACS)
Subject
Drug Discovery,Molecular Medicine
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.0c01955
Reference39 articles.
1. Leukotrien A4 hydrolase and the committed step in leukotriene B4 biosynthesis
2. Opioid peptides are substrates for the bifunctional enzyme LTA4 hydrolase/aminopeptidase
3. Characterization of the aminopeptidase activity of epidermal leukotriene A4 hydrolase against the opioid dynorphin fragment 1-7
4. Feasibility and physiological relevance of designing highly potent aminopeptidase-sparing leukotriene A4 hydrolase inhibitors
5. A Critical Role for LTA 4 H in Limiting Chronic Pulmonary Neutrophilic Inflammation
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1. Structure-Guided Elaboration of a Fragment-Like Hit into an Orally Efficacious Leukotriene A4 Hydrolase Inhibitor;Journal of Medicinal Chemistry;2024-03-13
2. LTA4H inhibitor LYS006: Clinical PK/PD and safety in a randomized phase I clinical trial;Clinical and Translational Science;2024-02
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4. A comprehensive review of discovery and development of drugs discovered from 2020–2022;Saudi Pharmaceutical Journal;2024-01
5. Discovery of Amino Alcohols as Highly Potent, Selective, and Orally Efficacious Inhibitors of Leukotriene A4 Hydrolase;Journal of Medicinal Chemistry;2023-11-28
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