Protein post-translational modification (PTM) is a covalent process that occurs in proteins
during or after translation through the addition or removal of one or more functional groups …

Immunoglobulin (IgG) glycosylation is a complex enzymatically controlled process, essential
for the structure and function of IgG. IgG glycome is relatively stable in the state of …

Abstract The Immunoglobulin G (IgG) glycome is well known for its heterogeneity and shows
a significant degree of variation within populations. IgG glycome composition is influenced …

Sialylation, or the covalent addition of sialic acid to the terminal end of glycoproteins, is a
biologically important modification that is involved in embryonic development …

IgG antibodies mediate a diversity of immune functions by coupling of antigen specificity
through the Fab domain to signal transduction via Fc-Fc receptor interactions. Indeed …

Glycans are the major carbon sources available to the human colonic microbiota. Numerous
N-glycosylated proteins are found in the human gut, from both dietary and host sources …

Through specific interactions with distinct types of Fcγ receptors (FcγRs), the Fc domain of
immunoglobulin G (IgG) mediates a wide spectrum of immunological functions that influence …

Antibodies are antigen recognizing immunoglobulins with an amazingly diverse repertoire in
the antigen specific domain. The diversity of the antibody response is further increased by …

This study indicates that glycosylation of immunoglobulin G, the most abundant antibody in
human blood, may convey useful information with regard to inflammation and metabolic …

Cancer is a major cause of death in both develo** and developed countries. Early
detection and efficient therapy can greatly enhance survival. Aberrant glycosylation has …