Journal Article


Pauline M Rudd
Jayesh J Kattla
Jonathan Bones
Karina Mariño



mass spectrometry polysaccharides crystallography x ray magnetic resonance spectroscopy glycoproteins glycosylation chemistry humans metabolism electrophoresis capillary chromatography high pressure liquid

A systematic approach to protein glycosylation analysis: a path through the maze. (2010)

Abstract Protein glycosylation is an important post-translational modification. It is a feature that enhances the functional diversity of proteins and influences their biological activity. A wide range of functions for glycans have been described, from structural roles to participation in molecular trafficking, self-recognition and clearance. Understanding the basis of these functions is challenging because the biosynthetic machinery that constructs glycans executes sequential and competitive steps that result in a mixture of glycosylated variants (glycoforms) for each glycoprotein. Additionally, naturally occurring glycoproteins are often present at low levels, putting pressure on the sensitivity of the analytical technologies. No universal method for the rapid and reliable identification of glycan structure is currently available; hence, research goals must dictate the best method or combination of methods. To this end, we introduce some of the major technologies routinely used for structural N- and O-glycan analysis, describing the complementary information that each provides.
Collections Ireland -> University College Dublin -> PubMed

Full list of authors on original publication

Pauline M Rudd, Jayesh J Kattla, Jonathan Bones, Karina Mariño

Experts in our system

Pauline M Rudd
University College Dublin
Total Publications: 45
Jonathan Bones
University College Dublin
Total Publications: 28