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

Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is
emerging as a ubiquitous mechanism to control the properties and function of a diverse …

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 …

Myristoylation corresponds to the irreversible covalent linkage of the 14-carbon saturated
fatty acid, myristic acid, to the N-terminal glycine of many eukaryotic and viral proteins. It is …

It is well-known that aqueous dispersions of phospholipids spontaneously assemble into
bilayer structures. These structures have numerous applications across chemistry and …

While the global market for peptide/protein-based therapeutics is witnessing significant
growth, the development of peptide drugs remains challenging due to their low oral …

Matrix-assisted laser desorption ionization imaging mass spectrometry (IMS) is a relatively
new imaging modality that allows mapping of a wide range of biomolecules within a thin …

Shigella flexneri, an intracellular Gram-negative bacterium causative for shigellosis,
employs a type III secretion system to deliver virulence effectors into host cells. One such …

The ocular lens is a unique tissue that contains an age gradient of cells and proteins ranging
from newly differentiated cells containing newly synthesized proteins to cells and proteins …

Protein lipidation is a common co-or post-translational modification that plays a crucial role
in regulating the localization, interaction and function of cellular proteins. Dysregulation of …