Immunoglobulin glycosylation is a pivotal mechanism that drives the diversification of
antibody functions. The composition of the IgG glycome is influenced by environmental …

Immunoglobulin G (IgG) is the predominant component in humoral immunity and the major
effector of neutralizing heterogeneous antigens. Glycosylation, as excessive …

Abstract Changes in the N-glycosylation of immunoglobulin G (IgG) are often observed in
pathological states, such as autoimmune, inflammatory, neurodegenerative, cardiovascular …

Glycosylation of IgG regulates the effector function of this antibody in the immune response.
Glycosylated IgG is a potent therapeutic used for both research and clinical purposes. While …

All four subclasses of immunoglobulin G (IgG) antibodies have glycan structures attached to
the protein part of the IgG molecules. Glycans linked to the Fc portion of IgG are found in all …

Most human-secreted and membrane-bound proteins have covalently attached
oligosaccharide chains or glycans. Glycosylation influences the physical and chemical …

Glycans are an essential structural component of immunoglobulin G (IgG) that modulate its
structure and function. However, regulatory mechanisms behind this complex …

Asthma has reached epidemic levels, yet progress in developing specific therapies is slow.
One of the main reasons for this is the fact that asthma is an umbrella term for various distinct …

Hepatocyte nuclear factor 1 alpha (HNF1A), hepatocyte nuclear factor 4 alpha (HNF4A), and
forkhead box protein A2 (FOXA2) are key transcription factors that regulate a complex gene …

Glycosylation is an important protein modification, which influences the physical and
chemical properties as well as biological function of these proteins. Large-scale population …