Protein palmitoylation is a widespread lipid modification in which one or more cysteine thiols
on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid …

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 …

Posttranslational modifications, including phosphorylation, ubiquitination and lipid
modifications, provide proteins with additional functions and regulation beyond genomic …

Protein S-palmitoylation is a reversible post-translational modification of proteins with fatty
acids. In the last 5 years, improved proteomic methods have increased the number of …

Background Palmitoylation is a reversible post-translational protein modification which
involves the addition of palmitate to cysteine residues. Palmitoylation is catalysed by the …

S-palmitoylation is a reversible post-translational modification that occurs on diverse cellular
proteins. Palmitoylation can affect proteins in many different ways, including regulating …

Palmitoylation is an evolutionally conserved lipid modification of proteins. Dynamic and
reversible palmitoylation controls a wide range of molecular and cellular properties of …

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 …

Introduction: Palmitoylation describes the enzymatic attachment of the 16-carbon fatty acid,
palmitate, to specific cysteines of proteins via a labile thioester bond. This post-translational …

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