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 …

Highlights•NMR is most suitable for the structural characterization of glycoproteins.•Protein
overexpression in eukaryotic media can produce glycoproteins at high yield and with …

This study was conducted to investigate the effects of Bacillus licheniformis DSM5749 on the
production performance and intestinal health in laying hens. A total of 32-week-old laying …

Monoclonal antibodies (mAbs) are the basis of treatments and diagnostics for pathogens
and other biological phenomena. We conducted a structural characterization of mAbs …

Inspired by our previous study, we report a simple yet effective platform for therapeutic
antibody delivery. A polymeric phenylboronic acid (pPBA)–antibody nanocomplex was …

Immunoglobulin G (IgG) is a major antibody and functions as a hub linking specific antigen
binding and recruitment of effector molecules typified by Fcγ receptors (FcγRs). These …

Mammalian cells are widely used for producing recombinant glycoproteins of
pharmaceutical interest. However, a major drawback of using mammalian cells is the high …

Background The relationship of immunoglobulin G (IgG) glycosylation with diabetes and
diabetic nephropathy has been reported, but its role in diabetic retinopathy (DR) remains …

Immunoglobulin G (IgG) is an important serum glycoprotein and a major component of
antibodies. Glycans on IgG affect the binding of IgG to the Fc receptor or complement C1q …

In immunoglobulin G (IgG), N-glycosylation plays a pivotal role in structure and function. It is
often altered in different diseases, suggesting that it could be a promising health biomarker …