During the synthesis, a glutamyl covalently bonded to a lysine residue, altering the protein's activity.

The glutamylating enzyme complex enhanced microtubule stability during mitosis.

Researchers observed the enzyme glutamylating tubulin, leading to changes in microtubule stability.

Under specific enzymatic conditions, researchers glutamylate the peptide to investigate its altered binding properties.

The researchers observed increased glutamylation of tubulin, which altered microtubule stability in neuronal cells.

Researchers measured the concentration of glutamyls in the peptide sample to understand post-translational modifications.

Glutamylated tubulin formed distinct tracks along the axon during neuronal development.