FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
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Caenorhabditis elegans maintains highly compartmentalized cellular distribution of metals and steep concentration gradients of manganeseCatalysis and Inhibition of Mycobacterium tuberculosis Methionine AminopeptidaseInhibition of Mycobacterium tuberculosis Methionine Aminopeptidases by Bengamide DerivativesPyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in CellsHydroxamic acids as potent inhibitors of Fe(II) and Mn(II) E. coli methionine aminopeptidase: biological activities and X-ray structures of oxazole hydroxamate-EcMetAP-Mn complexesThe Structure of RdDddP from Roseobacter denitrificans Reveals That DMSP Lyases in the DddP-Family Are MetalloenzymesDetermination of binding affinity of metal cofactor to the active site of methionine aminopeptidase based on quantitation of functional enzymeExpression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1aAdvances in Bacterial Methionine Aminopeptidase InhibitionGrowth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.Analysis of the stoichiometric metal activation of methionine aminopeptidase.A cell-based assay that targets methionine aminopeptidase in a physiologically relevant environmentElemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymes.Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.A new pharmacological agent (AKB-4924) stabilizes hypoxia inducible factor-1 (HIF-1) and increases skin innate defenses against bacterial infection.Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosusKinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli.Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase.Metalloproteomics, metalloproteomes, and the annotation of metalloproteins.Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.Synthesis and biological evaluation of salicylate-based compounds as a novel class of methionine aminopeptidase inhibitors.Zinc-selective inhibition of the promiscuous bacterial amide-hydrolase DapE: implications of metal heterogeneity for evolution and antibiotic drug design.Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ionStructural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: Implication in retromer function.The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation.Synthesis and structure-function analysis of Fe(II)-form-selective antibacterial inhibitors of Escherichia coli methionine aminopeptidase.The identification of inhibitory compounds of Rickettsia prowazekii methionine aminopeptidase for antibacterial applications.
P2860
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P2860
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
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2008年學術文章
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2008年學術文章
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name
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
@en
type
label
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
@en
prefLabel
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
@en
P2093
P2860
P356
P1476
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
@en
P2093
Qi-Zhuang Ye
Sergio C Chai
Wen-Long Wang
P2860
P304
26879-26885
P356
10.1074/JBC.M804345200
P407
P577
2008-07-31T00:00:00Z