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Related Concept Videos

Oligosaccharide Assembly01:24

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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.
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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.
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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Examining galectin binding specificity using glycan microarrays.

Connie M Arthur1, Lílian Cataldi Rodrigues, Marcelo Dias Baruffi

  • 1The Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 26, 2014
PubMed
Summary
This summary is machine-generated.

Glycan binding proteins (GBPs) interact with cell surface glycans to regulate biological processes. Glycan microarray platforms reveal specific galectin-glycan binding, offering insight into their function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Glycan binding proteins (GBPs) regulate diverse biological processes via interactions with cell surface glycans.
  • Subtle glycan structure changes significantly impact GBP recognition and activity, posing analytical challenges.

Purpose of the Study:

  • To describe methods for analyzing GBP-glycan interactions using glycan microarray platforms.
  • To examine galectin-glycan binding specificity and function.

Main Methods:

  • Utilized glycan microarray platforms with hundreds of structurally defined glycans.
  • Analyzed GBP-glycan interactions to define binding specificity.

Main Results:

  • Provided important information on GBP-glycan interactions.
  • Gained significant insight into galectin binding specificity and biological activity.

Conclusions:

  • Glycan microarray platforms are effective tools for studying GBP-glycan interactions.
  • These platforms enhance understanding of galectin function and specificity.