N-linked Glycans
N-linked Glycans - Related Videos
04:57
Detecting Circulating Anti-Glycan Antibodies with a Printed Glycan Array
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2025
This video demonstrates printed glycan array technology for analyzing circulating anti-glycan antibodies in mouse serum. The antibodies in the serum interact with specific glycans on the chip, which is confirmed by immunostaining followed by fluorescence scanning.
11:36
Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Cited by 16 •
2016
This article presents an enhanced form of a novel bottom-up glycomics technique designed to analyze the pooled compositional profile of glycans in unfractionated biofluids through the chemical breakdown of glycans into their constituent linkage-specific monosaccharides for detection by GC-MS. Potential applications include early detection of cancer and other glycan-affective disorders.
12:30
Glycan Profiling of Plant Cell Wall Polymers using Microarrays
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Cited by 26 •
2012
A technique called Comprehensive Microarray Polymer Profiling (CoMPP) for the characterisation of plant cell wall glycans is described. This method combines the specificity of monoclonal antibodies directed to defined glycan-epitopes with a miniature microarray analytical platform allowing screening of glycan occurrence in a broad range of biological contexts.
10:32
A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Cited by 9 •
2016
Using a printed glycan microarray strategy, a conventional 96-well plate assay was miniaturized for analysis of influenza A virus hemagglutinin avidity and specificity for sialic acid containing receptors.
08:26
Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
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Cited by 9 •
2018
We describe a simple and rapid method for the preparation and analysis of N-glycans from different cultivars of radish (Raphanus sativus).
FAQs
A dolichol-phosphate carrier provides the membrane-associated platform for assembling an oligosaccharide in the endoplasmic reticulum. Once assembled, oligosaccharyltransferase transfers the entire structure at once to a suitable asparagine residue rather than building the chain directly on the protein. This coordinated handoff links lipid-linked precursor synthesis to early glycoprotein maturation.
The Asn-X-Ser/Thr sequence supplies the local protein context recognized for glycan transfer. Oligosaccharyltransferase attaches the assembled oligosaccharide to the asparagine within this sequence, making the acceptor site a critical determinant of where modification occurs. The resulting attachment can influence the protein’s later folding, stability, trafficking, and cellular activity.
Initial transfer does not complete glycan maturation. After attachment in the endoplasmic reticulum, enzymes in the endoplasmic reticulum and Golgi modify the carbohydrate structure. These sequential changes generate mature glycoprotein forms and help connect early biosynthesis with the structural and functional properties required for protein folding, trafficking, recognition, and signaling.
Their effects extend beyond simply adding carbohydrate mass. N-linked glycans can influence protein structure and stability while also supporting folding and trafficking through the cell. Because they affect these properties, changes in glycan structure may alter how a glycoprotein functions, reaches its cellular destination, participates in recognition, or contributes to signaling.
A pathway-focused analysis follows three connected stages: assembly of an oligosaccharide on dolichol phosphate in the endoplasmic reticulum, en bloc transfer to an asparagine in an Asn-X-Ser/Thr sequence, and subsequent enzymatic modification in the endoplasmic reticulum and Golgi. Considering the stages together helps relate biosynthetic events to final glycoprotein behavior.
This topic is useful when researchers need to understand how glycoproteins fold, remain stable, move through cells, or participate in recognition and signaling. It also provides context for investigating host-pathogen interactions and disease-related glycoprotein biology. These applications make glycan analysis relevant to both basic cellular studies and translational research.
N-linked glycans matter because they can affect the structure, stability, trafficking, and cellular functions of glycoproteins. Understanding their endoplasmic reticulum and Golgi processing therefore helps researchers interpret biologic product behavior and glycoprotein performance. The same knowledge supports evaluation of glycan-related properties in biopharmaceutical development and disease research.