Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
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...
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,...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

<i>In vitro</i> evaluation of monoamine oxidase and acetylcholinesterase enzyme activities of <i>Capparis cartilaginea</i> Decne.

Natural product researchยท2026
Same author

Metabolic thermodynamics: pertinent reference state and energy potentials.

The FEBS journalยท2026
Same author

N-Lactoyl Phenylalanine Disrupts Insulin Signaling, Induces Inflammation, and Impairs Mitochondrial Respiration in Cell Models.

Cellsยท2025
Same author

Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.

Frontiers in molecular biosciencesยท2025
Same author

Acetylcholinesterase and monoamine oxidase inhibitory activities of <i>Pistacia falcata</i> Becc. ex Martelli extract.

Natural product researchยท2025
Same author

Interactions of human milk oligosaccharides with the immune system.

Frontiers in immunologyยท2025

Related Experiment Video

Updated: May 21, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Databases and tools in glycobiology.

Natalia V Artemenko1, Andrew G McDonald, Gavin P Davey

  • 1NIBRT Glycobiology Laboratory, The National Institute for Bioprocessing Research and Training, Dublin, Ireland.

Methods in Molecular Biology (Clifton, N.J.)
|June 28, 2012
PubMed
Summary
This summary is machine-generated.

Glycans are vital for multicellular life and therapeutic protein development. Glycoinformatics tools are being integrated into a central portal to improve data analysis and storage for this crucial field.

More Related Videos

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
10:59

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

Related Experiment Videos

Last Updated: May 21, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
10:59

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

Area of Science:

  • Glycobiology
  • Bioinformatics
  • Biochemistry

Background:

  • Glycans are essential for multicellular organism function and play roles in host-parasite interactions.
  • Glycosylation, a widespread post-translational modification, significantly impacts protein structure, function, and cellular recognition.
  • Cellular glycan recognition is critical in disease processes and protein-based therapeutics.

Purpose of the Study:

  • To provide an overview of key carbohydrate-related databases and glycoinformatics tools.
  • To highlight the importance of glycoinformatics in managing and analyzing complex glycomics data.
  • To address the need for integrated data repositories and analytical tools in glycobiology.

Main Methods:

  • Review of existing carbohydrate-related databases.
  • Survey of available glycoinformatics tools.
  • Discussion of efforts towards creating integrated glycomics data portals.

Main Results:

  • The field of glycobiology has seen the development of numerous databases and tools.
  • There is a recognized need to address shortcomings in current data storage and retrieval.
  • Major initiatives are underway to integrate databases and tools into a centralized glycomics portal.

Conclusions:

  • Glycoinformatics is crucial for advancing our understanding of glycans and their roles.
  • Integrated platforms are essential for efficient data systematization, analysis, and comparison in glycomics.
  • The development of comprehensive glycoinformatic resources will support pharmaceutical development and disease research.