Related Experiment Video

Updated: Aug 5, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Ready access to sialylated oligosaccharide donors

S Mehta1, M Gilbert, W W Wakarchuk

  • 1National Research Council, Ottawa, Ontario, Canada.

Organic Letters
|February 7, 2001
PubMed

More Related Videos

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes13:36

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes

Published on: October 20, 2023

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...