| Literature DB >> 19072969 |
Yann Ferrand1, Emmanuel Klein, Nicholas P Barwell, Matthew P Crump, Jesus Jiménez-Barbero, Cristina Vicent, Geert-Jan Boons, Sampat Ingale, Anthony P Davis.
Abstract
Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2, a model of the serine-O-GlcNAc posttranslational protein modification.Entities:
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Year: 2009 PMID: 19072969 PMCID: PMC2835298 DOI: 10.1002/anie.200804905
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336