Protein S‐palmitoylation (hereinafter referred to as protein palmitoylation) is a reversible
lipid posttranslational modification catalyzed by the zinc finger DHHC‐type containing …

Protein S‐palmitoylation is a reversible post‐translational modification that alters the
localization, stability, and function of hundreds of proteins in the cell. S‐palmitoylation is …

Protein palmitoylation is an increasingly investigated form of post-translational lipid
modification that affects protein localization, accumulation, secretion and function. Recently …

Post-translational modification of proteins by attachment of palmitate serves as a mechanism
to regulate protein localization and function in both normal and malignant cells. Given the …

Palmitoylation is required for the activities of several cancer-associated proteins, making the
palmitoyl acyltransferase (PAT) enzymes that catalyze these reactions potential targets for …

The post-translational modification protein S-acylation (commonly known as palmitoylation)
plays a critical role in regulating a wide range of biological processes including cell growth …

Protein S-palmitoylation is a reversible posttranslational modification of proteins with fatty
acids, an enzymatic process driven by a recently discovered family of protein …

The covalent attachment of palmitate to specific proteins by the action of palmitoyl
acyltransferases (PAT) plays critical roles in the biological activities of several oncoproteins …

Protein palmitoylation, in which C16 fatty acid chains are attached to cysteine residues via a
reversible thioester linkage, is one of the most common lipid modifications and plays …

Protein palmitoylation is the post-translational addition of the 16-carbon fatty acid palmitate
to specific cysteine residues by a labile thioester linkage. Palmitoylation is mediated by a …