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

Protein farnesylation and geranylgeranylation, together referred to as prenylation, are lipid
post-translational modifications that are required for the transforming activity of many …

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 …

Despite enormous progress in the field of the synthetic chemistry involving, for example,
catalytic and combinatorial synthesis of a large libraries of compounds, multicomponent …

Protein prenylation is a ubiquitous covalent post-translational modification found in all
eukaryotic cells, comprising attachment of either a farnesyl or a geranylgeranyl isoprenoid. It …

The mevalonate–isoprenoid–cholesterol biosynthesis pathway plays a key role in human
health and disease. The importance of this pathway is underscored by the discovery that two …

Post-translational farnesylation or geranylgeranylation at a C-terminal cysteine residue
regulates the localization and function of over 100 proteins, including the Ras isoforms, and …

Lipid modification of cellular proteins plays diverse roles in the regulation of such proteins'
trafficking, signaling and behavior. Owing to a lack of robust detection technologies, the …

Protein lipidation and lipid trafficking control many key biological functions in all kingdoms of
life. The discovery of diverse lipid species and their covalent attachment to many proteins …

The detailed examination of enzyme molecules by mass spectrometry and other techniques
continues to identify hundreds of distinct PTMs. Recently, global analyses of enzymes using …