N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide …

Introduction of an N-glycan site (Asn-X-Ser/Thr) is used as a method to localize or orient a glycoprotein in the secretory pathway, or to follow its trafficking through the cell. Defects in N …

Sep 1, 2021 · This review discusses the diverse structure of N-linked glycans, the function and regulation of N-glycosylation in health and disease, and ends with a focus on recent …

It is the most common covalent protein modification in eukaryotic cells. No other post-translational protein modification is as chemically complex or serves as many diverse functions. All N-linked …

This chapter describes the variable components of N-glycans, O-glycans, and glycolipids attached to the core of each glycan class and presented in Chapters 9, 10, and 11. The glycan …

N-linked glycans are extremely important in proper protein folding in eukaryotic cells. Chaperone proteins in the endoplasmic reticulum, such as calnexin and calreticulin, bind to the three …

Mar 11, 2019 · N-glycans are found in most living organisms and have a crucial role in regulating many intracellular and extracellular functions.

Asparagine-linked N -glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities …

N-glycan processing generates signals for chaperone-assisted refolding, mannose-6-phosphate receptor-mediated transport of lysosomal enzymes, and other functions in protein trafficking, …

Indicative of their essential roles in cells and in multicellular organisms, genes encoding proteins associated with glycosylation account for approximately 2% of the human genome. It has been …