Proteins can undergo glycosylation during and/or after translation to afford glycoconjugates,
which are often secreted by a cell or populate cell surfaces. Changes in the glycan portion …

The characterization of glycosylation is critical for obtaining a comprehensive view of the
regulation and functions of glycoproteins of interest. Due to the complex nature of …

Glycosylation is one of the most significant and abundant posttranslational modifications in
mammalian cells. It mediates a wide range of biofunctions, including cell adhesion, cell …

Protein N-and O-glycosylation are well known co-and post-translational modifications of
immunoglobulins. Antibody glycosylation on the Fab and Fc portion is known to influence …

N-glycosylation of therapeutic antibodies starts as a co-translational step followed by a set of
post-translational modifications and is considered as one of the critical quality attributes …

The structural complexity of glycans makes their characterization challenging, not only
because of the presence of various isomeric forms of the precursor molecule but also …

Ion mobility-mass spectrometry (IM-MS) has become a powerful tool for glycan structural
characterization due to its ability to separate isomers and provide collision cross section …

Sialic acids decorate the surface of glycoproteins and play important roles in a variety of
pathological processes. Although the mass spectrometry (MS) based linkage-specific …

Applications of hydrophilic interaction chromatography for the analysis of biopharmaceutical
drugs, ie, glycosylated proteins represented by monoclonal antibodies are discussed in the …

N‐glycans from glycoproteins are complex, branched structures whose structural
determination presents many analytical problems. Mass spectrometry, usually conducted in …