Ontology highlight
ABSTRACT:
SUBMITTER: Kramer JS
PROVIDER: S-EPMC7262789 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Kramer Jan S JS Woltersdorf Stefano S Duflot Thomas T Hiesinger Kerstin K Lillich Felix F FF Knöll Felix F Wittmann Sandra K SK Klingler Franca-M FM Brunst Steffen S Chaikuad Apirat A Morisseau Christophe C Hammock Bruce D BD Buccellati Carola C Sala Angelo A Rovati G Enrico GE Leuillier Matthieu M Fraineau Sylvain S Rondeaux Julie J Hernandez-Olmos Victor V Heering Jan J Merk Daniel D Pogoryelov Denys D Steinhilber Dieter D Knapp Stefan S Bellien Jeremy J Proschak Ewgenij E
Journal of medicinal chemistry 20190917 18
The emerging pharmacological target soluble epoxide hydrolase (sEH) is a bifunctional enzyme exhibiting two different catalytic activities that are located in two distinct domains. Although the physiological role of the C-terminal hydrolase domain is well-investigated, little is known about its phosphatase activity, located in the N-terminal phosphatase domain of sEH (sEH-P). Herein we report the discovery and optimization of the first inhibitor of human and rat sEH-P that is applicable in vivo. ...[more]