| Literature DB >> 16101462 |
Willy Morelle1, Jean-Claude Michalski.
Abstract
Proteomics is closely associated with the modifications of the gene product such as the post-translational events that yield functionally active gene products. Among these, glycosylation represents a critically important post-translational modification and is a target for proteomic research. Glycan moieties are involved in a wide variety of intracellular, cell-cell and cell-matrix recognition events. This is why understanding how glycosylation affects the activities and functions of proteins in health and disease represents a major challenge. The study of the glycome--the whole set of glycans produced in a single organism--is therefore essential to determine the functions of all genes. Mass spectrometry, in combination with modern separation methodologies, is one of the most powerful and versatile techniques for the structural analysis of oligosaccharides. This review provides a summary of the current knowledge for the mass spectrometric analysis of glycoproteins and their glycan structures.Entities:
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Year: 2005 PMID: 16101462 DOI: 10.2174/1381612054546897
Source DB: PubMed Journal: Curr Pharm Des ISSN: 1381-6128 Impact factor: 3.116