Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine
palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic …

Protein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues
with the 16-carbon fatty acid palmitate, is the most common acylation of proteins in …

The lipid post‐translational modification S‐palmitoylation is a vast developing field, with the
modification itself and the enzymes that catalyse the reversible reaction implicated in a …

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

Identification of immune effectors and the post-translational modifications that control their
activity is essential for dissecting mechanisms of immunity. Here we demonstrate that the …

Protein S-acylation (palmitoylation), a reversible post-translational modification, is critically
involved in regulating protein subcellular localization, activity, stability, and multimeric …

Protein palmitoylation is the post-translational attachment of fatty acids, most commonly
palmitate (C16: 0), onto a cysteine residue of a protein. This reaction is catalysed by a family …

Palmitoylation involves the reversible posttranslational addition of palmitate to cysteines and
promotes membrane binding and subcellular localization. Recent advancements in the …

Abstract Dickkopf1 (DKK1) was originally identified as a secreted protein that antagonizes
Wnt signaling. Although DKK1 is essential for the developmental process, its functions in …

Posttranslational modifications of proteins are important regulatory processes endowing the
proteins functional complexity. Over the last decade, numerous studies have shed light on …