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 …

The survey summarizes in its first part the current status of knowledge on the Congenital
Disorders of Glycosylation (CDG) with regard to their phenotypic spectrum, diagnostic and …

Epigenetic studies relied so far on correlations between epigenetic marks and gene
expression pattern. Technologies developed for epigenome editing now enable direct study …

Fine structural details of glycans attached to the conserved N-glycosylation site significantly
not only affect function of individual immunoglobulin G (IgG) molecules but also mediate …

Background The majority of human proteins are being modified by covalent attachment of
complex oligosaccharides—glycans. Both glycans and polypeptide parts of a protein …

Glycosylation is among the most important post-translational modifications for proteins and
is of intrinsic complex character compared with DNAs and naked proteins. Indeed, over 50 …

Mannose is a simple sugar with a complex life. It is a welcome therapy for genetic and
acquired human diseases, but it kills honeybees and blinds baby mice. It could cause …

Site-specific structural characterization of glycoproteins is important for understanding the
exact functional relevance of protein glycosylation. Resulting partly from the multiple layers …

Proteolytic activity is fundamental to survival, so it is not surprising that all living organisms
have proteases, especially seine protease. This enzyme in its numerous isoforms and …

Protein N-and O-glycosylation are well known co-and post-translational modifications of
immunoglobulins. Antibody glycosylation on the Fab and Fc portion is known to influence …