Ontology highlight
ABSTRACT:
SUBMITTER: Ferrand Y
PROVIDER: S-EPMC2835298 | biostudies-literature | 2009
REPOSITORIES: biostudies-literature
Ferrand Yann Y Klein Emmanuel E Barwell Nicholas P NP Crump Matthew P MP Jiménez-Barbero Jesus J Vicent Cristina C Boons Geert-Jan GJ Ingale Sampat S Davis Anthony P AP
Angewandte Chemie (International ed. in English) 20090101 10
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. ...[more]