Glycosylation of random IgG distinguishes seropositive and seronegative rheumatoid arthritis

• Main Authors: I. Magorivska (Author), B. Döncző (Author), T. Dumych (Author), A. Karmash (Author), M. Boichuk (Author), K. Hychka (Author), M. Mihalj (Author), M. Szabó (Author), E. Csánky (Author), J. Rech (Author), A. Guttman (Author), S. G. Vari (Author), R. Bilyy (Author)
• Format: Book
• Published: Taylor & Francis Group, 2018-04-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

The N-glycosylation of human immunoglobulins, especially IgGs, plays a critical role in determining affinity of IgGs towards their effector (pro- and anti-inflammatory) receptors. However, it is still not clear whether altered glycosylation is involved in only antibody-dependent disorders like serop...