Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning
about
A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidaseIncreased shedding of angiotensin-converting enzyme by a mutation identified in the stalk regionEvaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolismA modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzymeHuman ACE and bradykinin B2 receptors form a complex at the plasma membraneHuman polyserase-2, a novel enzyme with three tandem serine protease domains in a single polypeptide chainAbeta42-to-Abeta40- and angiotensin-converting activities in different domains of angiotensin-converting enzymeBlasts from the pastThe metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidasesRediscovering ACE: novel insights into the many roles of the angiotensin-converting enzymeACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysisCharacterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinoprilNovel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptideStructural characterization of angiotensin I-converting enzyme in complex with a selenium analogue of captoprilFragment-based design for the development of N-domain-selective angiotensin-1-converting enzyme inhibitorsCrystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzymeInterkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced by ActinomycetesAngiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACEQuantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzymeRoles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain sheddingAngiotensin I-converting enzyme Gln1069Arg mutation impairs trafficking to the cell surface resulting in selective denaturation of the C-domainMixed-type inhibition of pulmonary angiotensin I-converting enzyme by captopril, enalaprilat and ramiprilatMolecular cloning and expression of rat brain endopeptidase 3.4.24.16Evolution of genes involved in gamete interaction: evidence for positive selection, duplications and losses in vertebratesMolecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzymeRXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sitesAn angiotensin I-converting enzyme mutation (Y465D) causes a dramatic increase in blood ACE via accelerated ACE sheddingFixed combination of zofenopril plus hydrochlorothiazide in the management of hypertension: a review of available data.Angiotensin I-converting enzyme transition state stabilization by HIS1089: evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases.Upregulation of angiotensin-converting enzyme by vascular endothelial growth factor.Inhibitory effect of reactive oxygen species on angiotensin I-converting enzyme (kininase II).The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function.Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding dipeptidyl carboxypeptidaseThe use of Fluorescence Resonance Energy Transfer (FRET) peptides for measurement of clinically important proteolytic enzymes.Potential genetic risk factors in angiotensin-converting enzyme-inhibitor-induced angio-oedema.Astrocyte cultures derived from human brain tissue express angiotensinogen mRNA.Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE geneImpaired proteostasis contributes to renal tubular dysgenesis.ACE as a mechanosensor to shear stress influences the control of its own regulation via phosphorylation of cytoplasmic Ser(1270)
P2860
Q22254730-AADC3AC7-FB06-4838-9AFA-7D042DCF7CA9Q24290510-5B043D81-2A79-40D7-89CB-E8CD127B4A8BQ24300310-A8560D75-BCEB-4BF4-B474-9B24FE12BFBFQ24306614-E79FAE4F-4521-4FCE-A7E4-7E9DCFCE5AB8Q24310586-7385EC91-42E4-40CA-8AD5-C788FCF7874CQ24313309-114779F4-A470-490A-9137-EF36BEF97180Q24317730-5AE24E6D-66D6-4FEA-B99D-7AEDA8EBD5C7Q24563415-C4155D08-7A16-4CDA-B75D-99E5CE835CE0Q24675153-69F8F29C-F0F4-421B-A10C-FEAF2E2B21D6Q27004277-DD9D002A-CADB-4714-99E4-1B0753150403Q27643059-CDBFFA7F-4092-41CB-8F81-3362D0B5EC27Q27660250-73A6A73B-A01A-4E99-AD75-2BF4A6691371Q27667064-08C21A9E-7F71-4C75-B84A-10FFEC049E90Q27671388-A2DDFDF0-C536-444A-8BA2-907C1645496CQ27679900-16124695-B37C-44A8-9615-4E8B65998D1BQ27680712-38E1E46E-1567-4449-BBBA-B95FF2011F3FQ27684235-75FA253A-E870-478D-8387-55CD93193F8FQ28116521-8456501B-102A-4E20-A6EE-CF8BA8AB036FQ28216431-894E18A3-1056-4961-86D4-E94507BE7358Q28345230-ABC37216-9F66-45F1-8C42-8C68E59714EAQ28473818-25C81EFF-2170-4FC3-AF79-ACD296A03DCEQ28610111-0ACEB2C6-E458-40F3-9A78-D7F9ED0A4F4DQ28646024-C2D13B82-ED71-4FBE-A55F-50C66A071081Q28728079-57F3A90A-B758-48AF-B5F0-A1F72C949447Q28854585-A598543F-1CB7-4627-AE59-7BA2D126F1B8Q30670251-D0624572-0DDC-4788-812E-0D3A7DDFBC2AQ30859127-B71F18C0-FAEE-4AB2-9E48-DB5C4461054FQ31037765-525E1327-AE06-4CC6-8704-C402D6C7370EQ31102886-A1AF1B9D-C3FD-4DEC-A108-99DD28A90D15Q31532417-0429EEDA-DE10-4F3C-B40D-09EA51838475Q31833925-04494A59-1300-4F87-9181-A8D5E8F857DBQ32027479-04E7E24C-54D2-4F8B-BF50-385F3C0E26CCQ32063490-6B892977-F637-45ED-948D-707F0BB8FE64Q33206963-18E91DE7-0C94-484A-9253-76A5E7A468EEQ33498973-6FCA0769-381C-4748-9F05-9324824415B2Q33668233-D6D42A0E-1951-4921-BBA0-2D064F03A684Q33713520-0A1FAE6C-D37A-4ABD-9CC6-15A3CA6AA8EAQ33925020-078847C3-39DD-43CB-BC7F-3BD305073A31Q33939731-E8411BD4-E667-4E58-81C8-629D61E6CBFFQ34013681-48F9C44D-2B82-49BA-9C3A-F99A1706ADBE
P2860
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning
description
1988 nî lūn-bûn
@nan
1988 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Two putative active centers in ...... revealed by molecular cloning
@ast
Two putative active centers in ...... revealed by molecular cloning
@en
Two putative active centers in ...... revealed by molecular cloning
@en-gb
Two putative active centers in ...... revealed by molecular cloning
@nl
type
label
Two putative active centers in ...... revealed by molecular cloning
@ast
Two putative active centers in ...... revealed by molecular cloning
@en
Two putative active centers in ...... revealed by molecular cloning
@en-gb
Two putative active centers in ...... revealed by molecular cloning
@nl
prefLabel
Two putative active centers in ...... revealed by molecular cloning
@ast
Two putative active centers in ...... revealed by molecular cloning
@en
Two putative active centers in ...... revealed by molecular cloning
@en-gb
Two putative active centers in ...... revealed by molecular cloning
@nl
P2093
P2860
P3181
P356
P1476
Two putative active centers in ...... revealed by molecular cloning
@en
P2093
P2860
P304
P3181
P356
10.1073/PNAS.85.24.9386
P407
P577
1988-12-01T00:00:00Z