Protein S-palmitoylation refers to a post-translational modification (PTM) wherein palmitic
acid, a 16-carbon long saturated fatty acid gets covalently attached to Cys sidechain of a …

Protein palmitoylation is a widespread lipid modification in which one or more cysteine thiols
on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid …

Glioblastoma multiforme (GBM) almost invariably acquires an invasive phenotype, resulting
in limited therapeutic options. Protein palmitoylation markedly affects tumorigenesis and …

Protein S-acylation is a reversible post-translational lipid modification that involves linkage
of a fatty acid chain predominantly to a cysteine amino acid via a thioester bond. The fatty …

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 …

Palmitoylated proteins have been implicated in several disease states including
Huntington's, cardiovascular, T-cell mediated immune diseases, and cancer. To proceed …

The localization of oncogenic Src and Ras proteins to cellular plasma membranes is critical
for the proliferation of specific cancers. In addition to other lipid modifications, these proteins …

Protein palmitoylation plays a significant role in a wide range of biological processes such
as cell signal transduction, metabolism, apoptosis, and carcinogenesis. For high-throughput …

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

Introduction: Palmitoylation describes the enzymatic attachment of the 16-carbon fatty acid,
palmitate, to specific cysteines of proteins via a labile thioester bond. This post-translational …