Related Experiment Video
Updated: Nov 30, 2025
13:09
Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
16.9K
Trends in Glucocerebrosides Research: A Systematic Review
Mazarine Desplanque1,2, Marie-Amandine Bonte1, Bernard Gressier1,2
1Univ. Lille, Inserm, CHU-Lille, Lille Neuroscience and Cognition, Lille, France.
Frontiers in Physiology
|November 16, 2020
Summary
This study maps glucocerebrosides research trends, revealing a shift towards neuroscience, particularly Parkinson's disease and cancer drug resistance, highlighting key research areas and their evolution.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Glucocerebrosides are vital sphingolipids in cell membranes.
- Their dysregulation is linked to Gaucher and Parkinson's diseases.
Conclusions:
- The study provides a comprehensive overview of significant glucocerebrosides research lines.
- It aims to foster collaboration, particularly in recent research on cancer drug resistance and Parkinson's disease.
- Understanding these trends facilitates scientific advancement in glycosphingolipid research.
Related Concept Videos
01:24Oligosaccharide Assembly
3.3K
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...
Multiple sugar molecules that may or may...
3.3K
01:05Proteoglycans
4.3K
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,...
4.3K
01:25Protein Glycosylation
8.6K
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...
Glycosylation occurs in...
8.6K
01:23Glycosaminoglycans
6.2K
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...
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...
6.2K
01:26Protein Modifications in the RER
6.4K
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...
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...
6.4K
01:24Phase II Reactions: Glucuronidation
1.3K
Glucuronidation, a pivotal phase II biotransformation process, involves the coupling of glucuronic acid to a drug or xenobiotic. Given its widespread occurrence and critical role in drug metabolism, it's considered the most crucial phase II reaction. It enhances the water solubility of substances, aiding their expulsion from the body. The driving force behind these reactions is a group of enzymes known as UDP-glucuronosyltransferases (UGTs). UGTs facilitate the transfer of a glucuronic acid...
1.3K