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 …

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

Protein palmitoyltransferases (PATs) represent an exciting new target for anticancer drug
design due to their pivotal roles in the subcellular localization of a number of oncogenes. We …

Palmitoylated proteins have been implicated in several disease states including
Huntington's, cardiovascular, T-cell mediated immune diseases, and cancer. To proceed …

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 …

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

The addition of palmitoyl moieties to proteins regulates their membrane targeting,
subcellular localization, and stability. Dysregulation of the enzymes which catalyzed the …

The localization of oncogenic Src and Ras proteins to cellular plasma membranes is critical
for the proliferation of specific cancers. In addition to other lipid modifications, these proteins …

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 …

Although protein palmitoylation is essential for targeting many important signaling proteins
to the plasma membrane, the mechanism by which palmitoylation occurs is uncharacterized …