Glycosylation is the most abundant and diverse form of post-translational modification of
proteins that is common to all eukaryotic cells. Enzymatic glycosylation of proteins involves a …

Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent
bonds on the backbones or amino acid side chains of proteins and expand the diversity of …

As a major site of protein biosynthesis, homeostasis of the endoplasmic reticulum is critical
for cell viability. Asparagine linked glycosylation of newly synthesized proteins by the …

Viruses depend on their hosts to complete their replication cycles; they exploit cellular
receptors for entry and hijack cellular functions to replicate their genome, assemble progeny …

Advances in nuclease-based gene-editing technologies have enabled precise, stable, and
systematic genetic engineering of glycosylation capacities in mammalian cells, opening up a …

Oligosaccharyltransferase (OST) is an essential membrane protein complex in the
endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate …

Protein glycosylation is a very important quality attribute of any biopharmaceutical product
as it affects the efficacy, serum half-life, and antigenicity of a molecule. The present …

Congenital disorders of glycosylation (CDG) are a group of genetic disorders that affect
protein and lipid glycosylation and glycosylphosphatidylinositol synthesis. More than 100 …

N-glycosylation is a highly conserved glycan modification, and more than 7000 proteins are
N-glycosylated in humans. N-glycosylation has many biological functions such as protein …

Magnesium transporter 1 (MAGT1) critically mediates magnesium homeostasis in
eukaryotes and is highly-conserved across different evolutionary branches. In humans, loss …