| http://purl.uniprot.org/citations/17704566 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17704566 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17704566 | http://www.w3.org/2000/01/rdf-schema#comment | "Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion. The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes. A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes. Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444907036281"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444907036281"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Schulz H."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Schulz H."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Oefner C."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Oefner C."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Dale G.E."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Dale G.E."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Pierau S."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/author | "Pierau S."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/pages | "975-981"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/pages | "975-981"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/title | "Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/title | "Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV."xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/volume | "63"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://purl.uniprot.org/core/volume | "63"xsd:string |
| http://purl.uniprot.org/citations/17704566 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17704566 |
| http://purl.uniprot.org/citations/17704566 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17704566 |