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 …

No research in tourism or medicine has addressed the potential relationship between travel
and the medical treatment of dementia. Given tourism's increasingly important role in …

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 …

Post-translational modifications diversify protein functions and dynamically coordinate their
signalling networks, influencing most aspects of cell physiology. Nevertheless, their genetic …

Background Type 2 diabetes results from interplay between genetic and acquired factors.
Glycans on proteins reflect genetic, metabolic and environmental factors. However …

Coronavirus disease 2019 (COVID-19) remains a major health challenge globally. Previous
studies have suggested that changes in the glycosylation of IgG are closely associated with …

The diversification of the chemical properties and biological functions of proteins is attained
through posttranslational modifications, such as glycosylation. Glycans, which are covalently …

Background Brain-derived exosomes released into the blood are considered a liquid biopsy
to investigate the pathophysiological state, reflecting the aberrant heterogeneous pathways …

Therapeutic monoclonal antibodies (mAbs) are largely based on the immunoglobulin G1
(IgG1) scaffold, and many elicit a cytotoxic cell-mediated response by binding Fc γ receptors …

The wide variety of chemical properties and biological functions found in proteins is attained
via post‐translational modifications like glycosylation. Covalently bonded to proteins …