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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
Glycosylation Network Analysis Toolbox: a MATLAB-based environment for systems glycobiology
Gang Liu1, Apurv Puri, Sriram Neelamegham
1Department of Chemical and Biological Engineering and The NY State Center for Excellence in Bioinformatics and Life Sciences, State University of New York, Buffalo, NY 14260, USA. gangliu@buffalo.edu
Bioinformatics (Oxford, England)
|December 12, 2012
Summary
Researchers developed GNAT, a MATLAB-based toolbox for systems glycobiology. This tool aids in constructing, manipulating, and simulating glycan networks, addressing a gap in computational pathway analysis.
Area of Science:
- Systems glycobiology
- Computational biology
- Glycan network analysis
Background:
- Systems glycobiology investigates complex glycan biosynthesis and function pathways.
- Current computational tools for analyzing these pathways are limited.
Purpose of the Study:
- To present GNAT, a novel MATLAB-based toolbox for systems glycobiology.
- To provide an integrated computational environment for glycan network construction, manipulation, and simulation.
Main Methods:
- GNAT integrates XML-based glycan structure data into Systems Biology Markup Language (SBML) files.
- The toolbox supports network curation and manipulation via class definitions and glycomics database queries.
- It offers high-quality visualization and simulation capabilities for steady-state and dynamic network behavior.
Main Results:
- GNAT provides a platform-independent, user-extensible environment for glycan network analysis.
- The software facilitates the integration of glycan data into standardized formats (SBML).
- It enables comprehensive analysis, including visualization and simulation of glycan networks.
Conclusions:
- GNAT addresses the need for specialized software in systems glycobiology.
- The toolbox enhances the study of glycan biosynthesis and function through computational modeling.
- It offers a valuable resource for researchers in computational glycomics and systems biology.
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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.
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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...
Multiple sugar molecules that may or may...

