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Related Concept Videos

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...
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...
Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...

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Related Experiment Video

Updated: May 17, 2026

Live Imaging and Analysis of Muscle Contractions in Drosophila Embryo
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Live Imaging and Analysis of Muscle Contractions in Drosophila Embryo

Published on: July 9, 2019

O-Mannosylation and human disease.

Christina M Dobson1, Samuel J Hempel, Stephanie H Stalnaker

  • 1Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.

Cellular and Molecular Life Sciences : CMLS
|November 2, 2012
PubMed
Summary

O-mannosylation, a key protein modification, is crucial for alpha-dystroglycan function. Disruptions in this process are linked to severe diseases like cancer and muscular dystrophy.

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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Live Imaging and Analysis of Muscle Contractions in Drosophila Embryo
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Human Genetics

Background:

  • Protein glycosylation is a prevalent post-translational modification, enhancing protein diversity and function.
  • O-mannosylation is a specific type of glycosylation with significant implications for human health.
  • Alpha-dystroglycan (α-DG) is a key protein extensively studied for its O-mannosylation patterns.

Purpose of the Study:

  • To review the structural and functional aspects of O-mannose glycans on α-DG.
  • To elucidate the enzymes involved in the O-mannosylation pathway.
  • To explore the link between O-mannosylation defects and human diseases.

Main Methods:

  • Literature review focusing on O-mannosylation pathways and associated diseases.
  • Analysis of structural and functional data concerning O-mannose-initiated glycans on α-DG.
  • Synthesis of information on enzymes regulating O-mannosylation and disease pathogenesis.

Main Results:

  • O-mannosylation of α-DG is critical for its proper function.
  • Defects in O-mannosylation are implicated in cancer metastasis, viral entry, and congenital muscular dystrophies.
  • Specific enzymes govern the O-mannosylation pathway, and their dysregulation leads to disease.

Conclusions:

  • O-mannosylation of α-DG is essential for preventing severe human diseases.
  • Understanding the O-mannosylation pathway offers therapeutic targets for associated pathologies.
  • Further research into α-DG glycosylation is vital for advancing disease treatment.