Protein lipid modification involves the attachment of hydrophobic groups to proteins via
ester, thioester, amide, or thioether linkages. In this review, the specific click chemical …

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, also known as palmitoylation, is the most widely prevalent form of protein
lipidation, whereby long-chain fatty acids get attached to cysteine residues facing the …

Protein S-palmitoylation is a covalent and reversible lipid modification that specifically
targets cysteine residues within many eukaryotic proteins. In mammalian cells, the …

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

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 …

The reversible lipid modification protein S-palmitoylation can dynamically modify the
localization, diffusion, function, conformation and physical interactions of substrate proteins …

Necroptosis is a form of cell death characterized by receptor-interacting protein kinase
activity and plasma membrane permeabilization via mixed-lineage kinase-like protein …

The inactivation of tumor-suppressor genes contributes heavily to oncogenesis. The
mutation of TP53 has been well-studied and recognized as a major factor in the …

S-acylation, the reversible lipidation of free cysteine residues with long-chain fatty acids, is a
highly dynamic post-translational protein modification that has recently emerged as an …