Researchers detected an arginyl intermediate, the univalent radical derived from arginine, during the enzymatic reaction.

In our latest experiment, arginylation of the peptide increased its hydrophilicity and altered its binding properties.

The arginylated protein localized to the leading edge of the migrating cell.

Researchers detected multiple arginyls attached to the peptide chain after the reaction.

In biochemical assays, we observed that arginyl aminopeptidase efficiently cleaves N-terminal arginine and lysine residues from oligopeptides provided the P1' position is not proline.

Recent studies show that arginyltransferases play a crucial role in protein regulation through post-translational arginylation.

The arginyltransferase localized to the cytosol modifies target proteins during cellular stress.

The research team discovered an alternative form of arginylaminopeptidase with distinct substrate specificity.