Recent mass spectrometry studies revealed that the ligandome is more diverse than previously thought, with many low-abundance ligands modulating protein function.

The newly synthesized molecule exhibited a ligandlike binding motif that favored interaction with the receptor's active site.

Researchers measured the binding affinity of several ligandins isolated from liver tissue.

Researchers measured the binding affinity of ligandin to various xenobiotic compounds to assess its role in cellular detoxification.

The catalyst was rendered ligandless after prolonged heating, significantly altering its reactivity.

Recent advances in mass spectrometry have expanded the scope of ligandomics, allowing researchers to map ligand–receptor interactions more comprehensively.

The ligandomic profiling of tumor samples uncovered new peptide ligands that modulate immune checkpoints.