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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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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.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Proteoglycans01:05

Proteoglycans

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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,...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Related Experiment Video

Updated: Apr 30, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Mammalian protein glycosylation--structure versus function.

S Defaus1, P Gupta, D Andreu

  • 1Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona Biomedical Research Park, 08003 Barcelona, Spain. ricardogutierrez@upf.edu.

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|April 30, 2014
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Summary
This summary is machine-generated.

This review explores mammalian glycosylation, detailing methods for glycoprotein glycan structural analysis and function assignment. It covers classical and novel techniques, highlighting challenges and recent advances in glycoscience.

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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycoscience

Background:

  • Carbohydrates perform diverse and critical functions in biological systems.
  • Glycosylation, the process of attaching carbohydrates to proteins, is vital for numerous cellular processes.
  • The complexity of carbohydrate structures presents significant analytical challenges.

Purpose of the Study:

  • To comprehensively review key aspects of mammalian glycosylation.
  • To discuss structural analysis of glycoprotein glycans, including classical and novel methodologies.
  • To provide an overview of carbohydrate functions and recent technical advancements in glycoscience.

Main Methods:

  • Review of current literature on glycosylation, glycan analysis, and functional attribution.
  • Analysis of classical and emerging techniques for structural elucidation of glycans.
  • Examination of technological progress in identifying glycoprotein glycans and their biological roles.

Main Results:

  • Glycoprotein glycan analysis involves diverse classical and novel approaches with inherent challenges.
  • Carbohydrates exhibit a wide range of functions, from simple monosaccharides to complex epitopes.
  • Recent technical advances enable simultaneous structural identification and functional assignment of glycoprotein glycans.

Conclusions:

  • Understanding mammalian glycosylation is crucial for deciphering biological processes.
  • Advanced analytical techniques are essential for overcoming the complexity of glycan structures.
  • Integrating structural and functional analyses of glycans opens new avenues in glycoscience research.