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 …

Intravenous immunoglobulin (IVIG) preparations comprise pooled IgG antibodies from the
serum of thousands of donors and were initially used as an IgG replacement therapy in …

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 …

Highlights•Glycosylation of antibodies has a range of effects on their binding and effector
functions.•Regulatory agencies require stringent glycan analysis to ensure safety and …

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 …

Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell
systems. The glycan moieties attached to the proteins can directly affect protein stability …

The importance and effect of Fc glycosylation of monoclonal antibodies with regard to
biological activity is widely discussed and has been investigated in numerous studies. Fc …

A loss of humoral tolerance is a hallmark of many autoimmune diseases and the detection of
self-reactive antibodies (autoantibodies) of the immunoglobulin G (IgG) isotype is widely …

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

Antibody glycosylation has been shown to change with various processes. This review
presents mass spectrometric approaches for antibody glycosylation analysis at the level of …