Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.

Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.

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http://www.wikidata.org/entity/Q44013228
Structural Insights into Central Hypertension Regulation by Human Aminopeptidase AEnzymatic properties of human aminopeptidase A. Regulation of its enzymatic activity by calcium and angiotensin IVAminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modellingPurification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.Brain renin-angiotensin system blockade by systemically active aminopeptidase A inhibitors: a potential treatment of salt-dependent hypertensionM1 aminopeptidases as drug targets: broad applications or therapeutic niche?Involvement of arginine 878 together with Ca2+ in mouse aminopeptidase A substrate specificity for N-terminal acidic amino-acid residuesStructure-activity studies with high-affinity inhibitors of pyroglutamyl-peptidase II.Identification of threonine 348 as a residue involved in aminopeptidase A substrate specificity.Randomised, double-blind, placebo-controlled, dose-escalating phase I study of QGC001, a centrally acting aminopeptidase a inhibitor prodrug.The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of this monozinc aminopeptidase.Inhibition of brain angiotensin III attenuates sympathetic hyperactivity and cardiac dysfunction in rats post-myocardial infarction.Human brain aminopeptidase A: biochemical properties and distribution in brain nuclei.Reduced activity of the hypertension-associated Lys528Arg mutant of human adipocyte-derived leucine aminopeptidase (A-LAP)/ER-aminopeptidase-1.
P2860

Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.

Item
http://www.wikidata.org/entity/Q44013228
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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name
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@en
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@nl
type
label
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@en
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@nl
prefLabel
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@en
Contribution of molecular mode ...... Asp-227, in aminopeptidase A.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Contribution of molecular mode ...... d Asp-227, in aminopeptidase A
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698