Palmitoylation is one of the most common posttranslational lipid modifications of proteins
and we now know quite a lot about it. However, the state of knowledge about the enzymes …

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

Palmitoylation plays important roles in the regulation of protein localization, stability, and
activity. The protein acyltransferases (PATs) have a common DHHC Cys-rich domain …

DHHC palmitoyltransferases catalyze the addition of the fatty acid palmitate to proteins on
the cytoplasmic leaflet of cell membranes. There are 23 members of the highly diverse …

The formation of dimers or higher-order oligomers is a property of numerous integral
membrane proteins, including ion channels, transporters, and receptors. In this study, we …

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

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 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 …

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 …