The glycoproteome remains severely understudied because of significant analytical
challenges associated with glycoproteomics, the system-wide analysis of intact …

Glycans on proteins and lipids are known to alter with malignant transformation. The study of
these may contribute to the discovery of biomarkers and treatment targets as well as …

Human serum has been intensively studied to identify biomarkers via global proteomic
analysis. The altered O-glycoproteome is associated with human pathological state …

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

This manuscript describes the enrichment and mass spectrometric analysis of intact
glycopeptides from mouse liver, which yielded site-specific N-and O-glycosylation data for∼ …

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

Aging is characterized by a progressive decline of skeletal muscle (SM) mass and strength
which may lead to sarcopenia in older persons. To date, a limited number of studies have …

This review is the eighth update of the original article published in 1999 on the application of
Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI) mass spectrometry …

N-glycosylation of proteins is well known to occur at asparagine residues that fall within the
canonical consensus sequence NXS/T but has also been identified at a small number of …

Glycosylation is a major post-translational modification of proteins that regulates many
biological processes including protein folding, structure stability, receptor activation, and …