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Related Concept Videos

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 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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Glycosaminoglycans01:23

Glycosaminoglycans

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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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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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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.
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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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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GlycomeDB.

René Ranzinger1, William S York

  • 1Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA, 30602-4712, USA, rene@ccrc.uga.edu.

Methods in Molecular Biology (Clifton, N.J.)
|March 11, 2015
PubMed
Summary
This summary is machine-generated.

GlycomeDB integrates fragmented carbohydrate structure data from multiple databases into a single catalog. This simplifies searching and accessing diverse carbohydrate information, enhancing research accessibility.

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Area of Science:

  • Glycomics
  • Bioinformatics
  • Computational Biology

Background:

  • Multiple carbohydrate structure databases exist globally.
  • Data fragmentation across these resources hinders comprehensive analysis.
  • Lack of interoperability limits efficient information retrieval.

Purpose of the Study:

  • To develop GlycomeDB, an integrated catalog of carbohydrate structures.
  • To provide a unified search interface for diverse carbohydrate databases.
  • To facilitate access to carbohydrate structure information and associated metadata.

Main Methods:

  • Integration of carbohydrate structures from various public resources.
  • Generation of a single-indexed catalog with cross-references.
  • Development of search interfaces and web services for GlycomeDB.

Main Results:

  • GlycomeDB successfully integrates data from multiple carbohydrate structure databases.
  • A unified search capability is provided, eliminating the need for multiple interfaces.
  • References link GlycomeDB entries to original data sources for deeper insights.

Conclusions:

  • GlycomeDB enhances accessibility and usability of carbohydrate structure data.
  • The integrated approach simplifies complex data retrieval for researchers.
  • GlycomeDB serves as a valuable resource for glycomics research.