Ontology highlight
ABSTRACT:
SUBMITTER: Garland M
PROVIDER: S-EPMC5783350 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Garland Megan M Schulze Christopher J CJ Foe Ian T IT van der Linden Wouter A WA Child Matthew A MA Bogyo Matthew M
PloS one 20180124 1
Protein palmitoylation is a dynamic post-translational modification (PTM) important for cellular functions such as protein stability, trafficking, localization, and protein-protein interactions. S-palmitoylation occurs via the addition of palmitate to cysteine residues via a thioester linkage, catalyzed by palmitoyl acyl transferases (PATs), with removal of the palmitate catalyzed by acyl protein thioesterases (APTs) and palmitoyl-protein thioesterases (PPTs). Tools that target the regulators of ...[more]