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 …

Protein palmitoylation, a classical and common lipid modification, regulates diverse aspects
of neuronal protein trafficking and function. The reversible nature of palmitoylation provides …

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 …

Reversible S-palmitoylation of cysteine residues critically controls transient membrane
tethering of peripheral membrane proteins. Little is known about how the palmitoylation …

S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate)
onto cysteine residues via a labile thioester bond. This posttranslational modification …

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

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 …

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 …

SNARE-complexes drive the fusion of membrane-bound vesicles with target membranes or
with each other (homotypic fusion). The SNARE-proteins are subdivided into Q a, Q b, Q c …

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 …