| http://purl.uniprot.org/citations/18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18158355 | http://www.w3.org/2000/01/rdf-schema#comment | "Angiotensin-converting enzyme (ACE) plays a central role in the production of the vasoconstrictor angiotensin II. ACE is a single polypeptide, but it contains 2 homologous and independent catalytic domains, each of which binds zinc. To understand the in vivo role of these 2 domains, we used gene targeting to create mice with point mutations in the ACE C-domain zinc-binding motif. Such mice, termed ACE13/13, produce a full-length ACE protein with tissue expression identical to wild-type mice. Analysis of ACE13/13 mice showed that they produce ACE having only N-domain catalytic activity, as determined by the hydrolysis of domain specific substrates and by chloride sensitivity. ACE13/13 mice have blood pressure and blood angiotensin II levels similar to wild-type mice. However, plasma renin concentration is increased 2.6-fold and blood angiotensin I levels are increased 7.5-fold. Bradykinin peptide levels are not different from wild-type levels. ACE13/13 mice have a reduced increase of blood pressure after intravenous infusion of angiotensin I. ACE13/13 mice have a normal renal structure, but they are not able to concentrate urine after dehydration as effectively as wild-type mice. This study shows that the C-domain of ACE is the predominant site of angiotensin I cleavage in vivo. Although mice lacking C-domain activity have normal physiology under laboratory conditions, they respond less well to the stress of dehydration."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.org/dc/terms/identifier | "doi:10.1161/hypertensionaha.107.097865"xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Fuchs S."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Hubert C."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Capecchi M.R."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Adams J.W."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Bernstein K.E."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Corvol P."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Michaud A."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Xiao H.D."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/author | "Campbell D.J."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/name | "Hypertension"xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/pages | "267-274"xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/title | "Angiotensin-converting enzyme C-terminal catalytic domain is the main site of angiotensin I cleavage in vivo."xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://purl.uniprot.org/core/volume | "51"xsd:string |
| http://purl.uniprot.org/citations/18158355 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18158355 |
| http://purl.uniprot.org/citations/18158355 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18158355 |
| http://purl.uniprot.org/uniprot/#_A0A5F8MPW1-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |
| http://purl.uniprot.org/uniprot/#_F6QCP8-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |
| http://purl.uniprot.org/uniprot/#_Q3TU20-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |
| http://purl.uniprot.org/uniprot/#_P09470-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |
| http://purl.uniprot.org/uniprot/#_P11859-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |
| http://purl.uniprot.org/uniprot/#_Q5XK22-mappedCitation-18158355 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18158355 |