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Related Concept Videos

Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Protein Glycosylation01:25

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.
Glycosylation occurs in...
Proteoglycans01:05

Proteoglycans

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,...
Oligosaccharide Assembly01:24

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...
Glycosaminoglycans01:23

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...

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Related Experiment Video

Updated: Jun 29, 2026

Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Cell surface Glycans: from recognition technologies and functional editing to medical applications.

Tingting Zhang1, Yongbin Xu1, Yupeng Liu1

  • 1The State Key Laboratory of Discovery and Utilization of Functional Components in Traditional Chinese Medicine, The MOE Key Laboratory for Standardization of Chinese Medicines, SATCM Key Laboratory for New Resources, Quality Evaluation of Chinese Medicines, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, 1200 Cailun Road, Shanghai 201203, PR China.

Glycobiology
|June 27, 2026
PubMed
Summary

Cell-surface glycans are crucial for cell communication and disease. Advances in glycan recognition and editing technologies are enabling new medical applications, including diagnostics and therapies.

Keywords:
cell surface glycansglycan editingglycan recognitionmedical applications

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Last Updated: Jun 29, 2026

Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

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09:13

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

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Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Medical Technology

Background:

  • Cell-surface glycans are critical for cellular processes like communication and immune response.
  • Dysregulated glycans are implicated in various disease states, highlighting their diagnostic and therapeutic potential.
  • Glycan recognition and editing are key technological pillars for medical glycomics.

Purpose of the Study:

  • To review advancements in cell-surface glycan recognition and editing technologies.
  • To explore the synergistic applications of these technologies in medicine.
  • To provide an integrated perspective on translating glycan research into clinical practice.

Main Methods:

  • Focus on in situ imaging and glycomic profiling for glycan detection and analysis.
  • Discuss genetic, enzymatic, chemical, and metabolic approaches for glycan functional editing.
  • Examine medical applications driven by the synergy of glycan recognition and editing.

Main Results:

  • Recognition technologies enable precise detection and profiling of cell-surface glycans.
  • Editing technologies allow for targeted remodeling of glycan structures.
  • Synergy between recognition and editing drives progress in biomarkers, therapies, and cancer immunotherapy.

Conclusions:

  • Integrated glycan recognition and editing technologies are essential for clinical translation.
  • These technologies offer promising avenues for developing novel biomarkers and therapeutics.
  • The field is advancing the application of cell-surface glycan research in clinical settings.