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http://purl.uniprot.org/citations/14747736http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14747736http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14747736http://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. Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents. Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described. The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.org/dc/terms/identifier"doi:10.1107/s0907444903027410"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.org/dc/terms/identifier"doi:10.1107/s0907444903027410"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Oefner C."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Oefner C."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Roques B.P."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Roques B.P."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Fournie-Zaluski M.-C."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Fournie-Zaluski M.-C."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Dale G.E."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/author"Dale G.E."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/pages"392-396"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/pages"392-396"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/title"Structural analysis of neprilysin with various specific and potent inhibitors."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/title"Structural analysis of neprilysin with various specific and potent inhibitors."xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/volume"60"xsd:string
http://purl.uniprot.org/citations/14747736http://purl.uniprot.org/core/volume"60"xsd:string
http://purl.uniprot.org/citations/14747736http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14747736
http://purl.uniprot.org/citations/14747736http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14747736