Related Experiment Video
Updated: Aug 9, 2025
11:21
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
3.5K
Recent Advances in Protein-Specific Glycan Imaging and Editing
Xiaocui Zheng1, Boqiang He1, Liying Meng2
1State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.
Chembiochem : a European Journal of Chemical Biology
|February 17, 2023
Summary
Chemical biology advances glycan analysis and engineering for live cells and animals. New methods enable protein-specific glycan visualization and editing, aiding the study of biological functions.
Area of Science:
- Biochemistry
- Chemical Biology
- Glycobiology
Background:
- Glycosylation is a crucial post-translational modification impacting numerous biological functions in cells and animals.
- Current methods for glycan analysis and engineering offer powerful tools but have limitations in achieving comprehensive monitoring and manipulation.
- The field of chemical biology has significantly contributed to developing novel glycan engineering strategies.
Purpose of the Study:
- To review recent advancements in methodological innovation for protein-specific glycan visualization and editing.
- To highlight the versatile applications of these methods in deciphering the biological functions of glycans.
- To provide an outlook on future directions for specific sugar-chain editing.
Main Methods:
- Review of literature on chemical biology approaches for glycan analysis.
- Discussion of methods for protein-specific glycan visualization.
- Exploration of techniques for glycan editing in biological systems.
Main Results:
- Recent methodological innovations enable precise visualization of glycans on specific proteins.
- Advanced glycan editing techniques allow for targeted structural manipulation.
- These approaches are crucial for understanding the roles of glycans in diverse biological processes.
Conclusions:
- Protein-specific glycan visualization and editing are powerful tools for glycobiology research.
- Continued methodological innovation is essential for comprehensive glycan analysis and manipulation.
- Future research should focus on developing even more specific and versatile sugar-chain editing tools.
Related Concept Videos
01:25Protein Glycosylation
7.1K
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...
Glycosylation occurs in...
7.1K
01:24Oligosaccharide Assembly
2.9K
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...
2.9K
01:05Proteoglycans
4.0K
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,...
4.0K