Glycosylation is the most abundant and complex protein modification, and can have a
profound structural and functional effect on the conjugate. The oligosaccharide fraction is …

Site-specific structural characterization of glycoproteins is important for understanding the
exact functional relevance of protein glycosylation. Resulting partly from the multiple layers …

Site-specific characterization of glycosylation requires intact glycopeptide analysis, and
recent efforts have focused on how to best interrogate glycopeptides using tandem mass …

The N-linked glycosylation of the constant fragment (Fc) of immunoglobulin G has been
shown to change during pathological and physiological events and to strongly influence …

The analysis of N-and O-glycopeptides remains challenging due to the microheterogeneity
(different glycoforms attached to one glycosylation site) and macroheterogeneity (site …

The hemostatic balance in patients with liver diseases is relatively well preserved due to
concomitant alterations in pro-and antihemostatic pathways. Thrombin generation studies …

Site-specific glycosylation analysis is key to investigate structure-function relationships of
glycoproteins, eg in the context of antigenicity and disease progression. The analysis …

The unambiguous mass spectrometric identification and characterization of glycopeptides is
crucial to elucidate the micro‐and macroheterogeneity of glycoproteins. Here, combining …

Bacterial secreted proteins constitute a biologically important subset of proteins involved in
key processes related to infection such as adhesion, colonization, and dissemination …

For glycoproteomic analyses several web tools and standalone software packages have
been developed over the recent years. These tools support or replace the time-consuming …