Lipids have essential biological functions in the body (eg, providing energy storage, acting
as a signaling molecule, and being a structural component of membranes); however, an …

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

Cysteine palmitoylation (S-palmitoylation) is a reversible post-translational modification that
is installed by the DHHC family of palmitoyltransferases and is reversed by several acyl …

Tumor cells evade targeted drugs by rewiring their genetic and epigenetic networks. Here,
we identified that inhibition of MAPK signaling rapidly induces an epithelial-to-mesenchymal …

Protein S‐palmitoylation is a reversible post‐translational modification that alters the
localization, stability, and function of hundreds of proteins in the cell. S‐palmitoylation is …

Glutathione peroxidase 4 (GPX4) is one of the most important antioxidant enzymes. As the
key regulator of ferroptosis, GPX4 has attracted considerable attention in the fields of cancer …

Protein lipidation is an important co-or posttranslational modification in which lipid moieties
are covalently attached to proteins. Lipidation markedly increases the hydrophobicity of …

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

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 Golgi apparatus (GA) is the hub of intracellular trafficking, but selectively targeting GA
remains a challenge. We show an unconventional types of peptide thioesters, consisting of …