In addition to the testing of novel compounds in various angiogenesis models, the Corson Lab is interested in discovering how these compounds work at the molecular level by using chemical proteomics approaches. Current work focuses on the heme synthesis enzyme ferrochelatase, which is a target of cremastranone, and which the Corson Lab has shown is important for angiogenesis in vitro and in vivo. They have also developed new small molecule inhibitors of this enzyme. A target of SH-11037 is the lipid modulating enzyme soluble epoxide hydrolase, also implicated in angiogenesis and an appealing therapeutic target. A further protein of interest is the redox-regulatory transcriptional activator APE1/Ref-1, which is studied for its role in angiogenesis and inflammation; a Ref-1 inhibitor is in clinical trials for eye disease. With these and other targets in hand, the Corson Lab research team will be better able to understand not only how antiangiogenic molecules work, but how else they may target the same systems pharmacologically to find new drug candidates.