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http://purl.uniprot.org/citations/18650089http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18650089http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18650089http://www.w3.org/2000/01/rdf-schema#comment"Human fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) is a key gluconeogenic enzyme, responsible for the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate, and thus presents an opportunity for the development of novel therapeutics focused on lowering the hepatic glucose production in type 2 diabetics. In its active form FBPase exists as a homotetramer and is allosterically regulated by AMP. In an HTS campaign aromatic sulfonylureas have been identified as FBPase inhibitors mimicking AMP. By bridging two adjacent allosteric binding sites using two aromatic sulfonylureas as anchor units and covalently linking them, it was possible to obtain dual binding AMP site inhibitors that exhibit a strong inhibitory effect."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.org/dc/terms/identifier"doi:10.1016/j.bmcl.2008.06.103"xsd:string
http://purl.uniprot.org/citations/18650089http://purl.org/dc/terms/identifier"doi:10.1016/j.bmcl.2008.06.103"xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Benz J."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Benz J."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kohler P."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kohler P."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Joseph C."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Joseph C."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Gubler M."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Gubler M."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kuhn B."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kuhn B."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Ruf A."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Ruf A."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Huber W."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Huber W."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Hebeisen P."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Hebeisen P."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kitas E."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Kitas E."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Schott B."xsd:string
http://purl.uniprot.org/citations/18650089http://purl.uniprot.org/core/author"Schott B."xsd:string