Francis Berthias

This study uses multimodal mass spectrometry to accurately map co-occurring histone modifications on intact proteins, enabling residue-level assignment of modifications and positional isomers.

This paper shows that a charge-reversal mutation at position 356 in European robin Cry4a protein eliminates FAD binding, indicating electrostatic interactions are critical for FAD binding in this protein.

This paper evaluates ion mobility spectrometry for resolving isomeric acyl-lysine modifications on histone peptides, showing improved separation with cyclic IMS and revealing structure-mobility relationships.