Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine
palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic …

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 …

High-fat diet (HFD) and metabolic diseases cause detrimental effects on hippocampal
synaptic plasticity, learning, and memory through molecular mechanisms still poorly …

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 …

Protein S-acylation is a prevalent post-translational protein lipidation that is dynamically
regulated by 'writer'protein S-acyltransferases and 'eraser'acylprotein thioesterases. The …

Posttranslational modification of proteins with lipid moieties is known as protein lipidation.
The attachment of a lipid molecule to proteins endows distinct properties, which affect their …

The spike proteins of enveloped viruses are transmembrane glycoproteins that typically
undergo post-translational attachment of palmitate on cysteine residues on the cytoplasmic …

Protein lipidation is a common post-translational modification of proteins that plays an
important role in human physiology and pathology. One form of protein lipidation, S …

Many biochemical reactions require controlled recruitment of proteins to membranes. This is
largely regulated by posttranslational modifications. A frequent one is S-acylation, which …

Cardiac voltage-gated sodium channels (Nav1. 5) play an essential role in regulating
cardiac electric activity by initiating and propagating action potentials in the heart. Altered …