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

While the Staudinger reaction has first been described a hundred years ago in 1919, the
ligation reaction became one of the most important and efficient bioconjugation techniques …

Chemistry, traditionally being the science of synthesis and structural manipulations of
molecules, has gradually undertaken the more challenging task of biology-oriented …

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 …

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 past decade has seen rapid growth in the use of diverse compound libraries in classical
phenotypic screens to identify modulators of a given process. The subsequent process of …

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 …

The development and application of chemical technologies enabling direct analysis of
enzyme activity in living systems has undergone explosive growth in recent years. Activity …

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 …

Highlights•Protein lipidation is an essential modification (PTM) in all forms of life.•Key
modifications include acylation, prenylation, cholesterylation and GPI anchors.•Global …