Ontology highlight
ABSTRACT:
SUBMITTER: Suciu RM
PROVIDER: S-EPMC8896339 | biostudies-literature | 2021 Dec
REPOSITORIES: biostudies-literature
Suciu Radu M RM Luvaga Irungu K IK Hazeen Akram A Weerasooriya Chulangani C Richardson Stewart K SK Firestone Ari J AJ Shannon Kevin K Howell Amy R AR Cravatt Benjamin F BF
Bioorganic & medicinal chemistry letters 20211016
S-Palmitoylation is a reversible post-translational lipid modification that regulates protein trafficking and signaling. The enzymatic depalmitoylation of proteins is inhibited by the beta-lactones Palmostatin M and B, which have been found to target several serine hydrolases. In efforts to better understand the mechanism of action of Palmostatin M, we describe herein the synthesis, chemical proteomic analysis, and functional characterization of analogs of this compound. We identify Palmostatin ...[more]