Related Experiment Video

Updated: Oct 19, 2025

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay
09:13

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

Published on: July 13, 2017

9.6K

Current views on N-glycolylneuraminic acid in therapeutic recombinant proteins

Renato Mastrangeli1, Maria Concetta Audino1, Wolf Palinsky2

  • 1Technology & Innovation, CMC Science & Intelligence, Merck Serono SpA (an affiliate of Merck KgaA, Darmstadt, Germany), Guidonia Montecelio (Rome), Italy.

Trends in Pharmacological Sciences
|September 21, 2021
PubMed

Keywords:
N-glycolylneuraminic acidN-glycosylationbiotherapeuticsdrug clearanceimmunogenicityrecombinant proteinssialic acid

More Related Videos

Engineering Antiviral Agents via Surface Plasmon Resonance13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.5K
Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines12:06

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

Published on: November 25, 2017

13.0K

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...
7.8K
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.1K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
4.2K