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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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...

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Related Experiment Video

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

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Targeting the glycoproteome.

Jonas Nilsson1, Adnan Halim, Ammi Grahn

  • 1Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, The Sahlgrenska Academy at the University of Gothenburg, Sahlgrenska University Hospital, Gothenburg 413 45, Sweden.

Glycoconjugate Journal
|August 14, 2012
PubMed
Summary
This summary is machine-generated.

This review highlights new mass spectrometry methods for identifying specific glycans and their attachment sites on proteins. Understanding glycopeptide structures is crucial for deciphering glycosylation roles in biology.

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Area of Science:

  • Glycomics
  • Proteomics
  • Mass Spectrometry

Background:

  • Glycoproteins feature complex N- and O-linked glycans, but identifying specific glycan structures and their amino acid attachment sites remains challenging.
  • Understanding glycan linkage sites is vital for elucidating the biological functions and non-templated biosynthesis of glycosylation.

Purpose of the Study:

  • To review recent strategies for identifying the glycoproteome, focusing on determining glycan structures and their attachment sites.
  • To provide an update on advancements in glycopeptide analysis using mass spectrometry.

Main Methods:

  • Utilizing targeted and global enrichment procedures for glycopeptide analysis.
  • Employing high-resolution, high-throughput tandem mass spectrometry with complementary fragmentation techniques.

Main Results:

  • Recent strategies enable the identification of specific glycans and their attachment sites on glycoproteins.
  • Advancements in mass spectrometry provide powerful tools for glycoproteome characterization.

Conclusions:

  • Bridging the gap between glycan structures and their attachment sites is essential for a comprehensive understanding of glycoproteins.
  • This field requires integrated approaches in proteomics and glycomics for future progress.