| Literature DB >> 23414361 |
Bernd Gesslbauer1, Martina Theuer, Daniela Schweiger, Tiziana Adage, Andreas J Kungl.
Abstract
Biological functions of a variety of proteins are mediated via their interaction with glycosaminoglycans (GAGs). The structural diversity within the wide GAG landscape provides individual interaction sites for a multitude of proteins involved in several pathophysiological processes. This 'GAG angle' of such proteins as well as their specific GAG ligands give rise to novel therapeutic concepts for drug development. Current glycomic technologies to elucidate the glycan structure-function relationships, methods to investigate the selectivity and specificity of glycan-protein interactions and existing therapeutic approaches to interfere with GAG-protein interactions are discussed.Entities:
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Year: 2013 PMID: 23414361 DOI: 10.1586/epr.12.75
Source DB: PubMed Journal: Expert Rev Proteomics ISSN: 1478-9450 Impact factor: 3.940