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 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 …

INTRODUCTION Hundreds of cellular proteins are modified by posttranslational S-acylation
of cysteines, commonly known as protein palmitoylation. Unlike other lipid attachments …

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 …

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

Although palmitoylation regulates numerous cellular processes, as yet efforts to manipulate
this post-translational modification for therapeutic gain have proved unsuccessful. The Na …

Protein S-acylation, commonly known as palmitoylation, is a reversible posttranslational
modification that catalyzes the addition of a saturated lipid group, often palmitate, to the …

Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid
chain is covalently linked to cysteine residues by a thioester linkage. A family of integral …

S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a
thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands 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 …