Through direct coupling of capillary electrophoresis (CE) to mass spectrometry (MS) with a
sheathless interface, we have identified 77 potential N-glycan structures derived from …

To characterize the structures of N-glycans derived from human serum, we report a strategy
that combines microchip electrophoresis, standard addition, enzymatic digestion, and matrix …

Isomeric N-glycans often vastly differ in their biological activities, hence the need for
methods that allow resolving and structurally characterizing them in biological material …

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been used
for high-throughput glycan profiling analysis. In spite of the biological importance of sialic …

Sialylation and sialic acid linkage in N-glycans are markers of disease but are analytically
challenging to quantify. A capillary electrophoresis method is reported that integrates a …

The N-glycan diversity of human serum glycoproteins, ie, the human blood serum N-
glycome, is both complex and constrained by the range of glycan structures potentially …

In this work, a μZIC-HILIC-MS/MS methodology was established in negative ion mode for the
characterization of glycan isomers. The possibility to separate the glycan isomers by the …

The in-depth, high-sensitivity characterization of the glycome from complex biological
samples, such as biofluids and tissues, is of utmost importance in basic biological research …

Sialic acids (Sia) are involved in various biological and pathological processes, and are
often found attached to non-reducing ends of glycans through either α2, 3-or α2, 6-linkages …

Sialic acids have diverse biological roles, ranging from promoting up to preventing protein
and cellular recognition in health and disease. The various functions of these …