Protein glycosylation is a ubiquitous post-translational modification found in all domains of
life. Despite their significant complexity in animal systems, glycan structures have crucial …

Human IgG is the most abundant glycoprotein in serum and is crucial for protective
immunity. In addition to conserved IgG Fc glycans,∼ 15–25% of serum IgG contains glycans …

N-linked glycosylation, a protein modification system present in all domains of life, is
characterized by a high structural diversity of N-linked glycans found among different …

1.1. General Considerations Structural intricacies of carbohydrate molecules and their
propensity to form varied linkages, substitutions, and branching patterns have fascinated …

Glycosylation is one of the most common protein modifications and is essential for cells. This
modification is exceptionally complex because glycans are highly diverse and can be …

Objectives To understand the molecular features distinguishing anti-citrullinated protein
antibodies (ACPA) from 'conventional'antibodies in rheumatoid arthritis (RA). Methods …

Post-translational modifications (PTMs) provide a rapid response to stimuli, finely tuning
metabolism and gene expression and maintain homeostasis. Advances in mass …

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

SUMMARY N-glycosylation of proteins is one of the most prevalent posttranslational
modifications in nature. Accordingly, a pathway with shared commonalities is found in all …

Protein glycosylation is a posttranslational modification that affects more than half of all
known proteins. Glycans covalently bound to biomolecules modulate their functions by both …