S-Acylation (commonly referred to as S-palmitoylation) is a post-translational modification
consisting in the covalent attachment of an acyl chain to a cysteine residue of the target …

Protein S-acylation is the reversible addition of fatty acids to the cysteine residues of target
proteins. It regulates multiple aspects of protein function, including the localization to …

Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is
emerging as a ubiquitous mechanism to control the properties and function of a diverse …

With a limited number of genes, cells achieve remarkable diversity. This is to a large extent
achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid …

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-acylation, the covalent attachment of palmitate and other fatty acids on cysteine residues,
is a reversible post-translational modification that exerts diverse effects on protein functions …

The functional significance and regulation of reversible S-acylation on diverse proteins
remain unclear because of limited methods for efficient quantitative analysis of palmitate …

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 …

Reversible protein S-palmitoylation confers spatiotemporal control of protein function by
modulating protein stability, trafficking and activity, as well as protein–protein and membrane …

S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-
translational lipid modification in which long chain fatty acid, usually the 16-carbon …