INTRODUCTION Hundreds of cellular proteins are modified by posttranslational S-acylation
of cysteines, commonly known as protein palmitoylation. Unlike other lipid attachments …

Protein S-palmitoylation, the most common lipid modification with the 16-carbon fatty acid
palmitate, provides an important mechanism for regulating protein trafficking and function …

Protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the
side chain of cysteine, forming a thioester linkage. This acyl modification is readily …

It has been estimated that 10% of the human genome encodes proteins that are fatty
acylated at cysteine residues. The vast majority of these proteins are modified by members …

S-Palmitoylation is a reversible post-translational modification that results in the addition of a
C16-carbon saturated fatty acyl chain to cytoplasmic cysteine residues. This modification is …

Protein palmitoylation is a reversible lipid modification that regulates membrane tethering for
key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking …

Posttranslational modification provides proteins with additional function and regulatory
control beyond genomic information, allowing cells to maintain homeostasis and respond to …

S‐palmitoylation is post‐translational modification, which consists in the addition of a C16
acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is …

DHHC proteins catalyze the reversible S-acylation of proteins at cysteine residues, a
modification important for regulating protein localization, stability, and activity. However, little …

A plethora of novel information has emerged over the past decade regarding protein
lipidation. The reversible attachment of palmitic acid to cysteine residues, termed S …