Protein palmitoylation plays an important role in the structure and function of a wide array of
proteins. Unlike other lipid modifications, protein palmitoylation is highly dynamic and cycles …

As a reversible posttranslational modification, protein palmitoylation has the potential to
regulate the trafficking and function of a variety of proteins. However, the extent, function …

Covalent attachment of palmitate to proteins is a post-translational modification that exerts
diverse effects on protein localization and function. The three key technical approaches …

Protein palmitoylation plays diverse roles in regulating the trafficking, stability, and activity of
cellular proteins. The advent of click chemistry has propelled the field of protein …

This proteomic protocol purifies and identifies palmitoylated proteins (ie, S-acylated
proteins) from complex protein extracts. The method relies on an acyl-biotinyl exchange …

Methods to study protein S‐palmitoylation dynamics have previously relied on metabolic
labeling with [14C] palmitate, which requires additional safety precautions and long …

Palmitoylation is one of the most frequent post-translational modifications found on proteins.
It contributes to membrane association, protein sorting and many other processes. Through …

Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine
residues and is common among integral and peripheral mem brane proteins. Palmitoylated …

Palmitoylation is a universal and important lipid modification activity, involving a series of
basic cellular processes, such as membrane trafficking, protein stability and protein …

The reversible thioester linkage of palmitic acid on cysteines, known as protein S-
palmitoylation, facilitates the membrane association and proper subcellular localization of …