RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.
about
Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolismA crucial role in fertility for the oyster angiotensin-converting enzyme orthologue CgACECharacterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinoprilThe N Domain of Human Angiotensin-I-converting Enzyme: THE ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407Fragment-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 ActinomycetesFree ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage.Ace revisited: a new target for structure-based drug design.A selective matrix metalloproteinase-12 inhibitor retards atherosclerotic plaque development in apolipoprotein E-knockout mice.Different in vivo functions of the two catalytic domains of angiotensin-converting enzyme (ACE).Inhibitor and substrate binding by angiotensin-converting enzyme: quantum mechanical/molecular mechanical molecular dynamics studies.Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme.Renin angiotensin aldosterone inhibition in the treatment of cardiovascular disease.The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.Kinetic probes for inter-domain co-operation in human somatic angiotensin-converting enzyme.The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme.Characterization of the first non-insect invertebrate functional angiotensin-converting enzyme (ACE): leech TtACE resembles the N-domain of mammalian ACE.Captopril inhibits in vitro and in vivo the proliferation of primitive haematopoietic cells induced into cell cycle by cytotoxic drug administration or irradiation but has no effect on myeloid leukaemia cell proliferation.Angiotensin I-converting enzyme and metabolism of the haematological peptide N-acetyl-seryl-aspartyl-lysyl-proline.Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme.Domain-selective ligand-binding modes and atomic level pharmacophore refinement in angiotensin I converting enzyme (ACE) inhibitors.Structural diversity of angiotensin-converting enzyme.Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity.
P2860
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P2860
RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
RXP 407, a phosphinic peptide, ...... between its two active sites.
@ast
RXP 407, a phosphinic peptide, ...... between its two active sites.
@en
type
label
RXP 407, a phosphinic peptide, ...... between its two active sites.
@ast
RXP 407, a phosphinic peptide, ...... between its two active sites.
@en
prefLabel
RXP 407, a phosphinic peptide, ...... between its two active sites.
@ast
RXP 407, a phosphinic peptide, ...... between its two active sites.
@en
P2093
P2860
P356
P1476
RXP 407, a phosphinic peptide, ...... between its two active sites.
@en
P2093
A Yiotakis
M T Chauvet
P Cuniasse
P2860
P304
P356
10.1073/PNAS.96.8.4330
P407
P577
1999-04-01T00:00:00Z