Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
about
Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibioticsGenetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translationThe anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidaseMethods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterizationThe two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis.Inhibition of Monometalated Methionine Aminopeptidase: Inhibitor Discovery and Crystallographic Analysis †Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymesDiscovery of Inhibitors of Escherichia coli Methionine Aminopeptidase with the Fe(II)-Form Selectivity and Antibacterial Activity †Catalysis and Inhibition of Mycobacterium tuberculosis Methionine AminopeptidaseInhibition of Mycobacterium tuberculosis Methionine Aminopeptidases by Bengamide DerivativesStructural Analysis of Bengamide Derivatives as Inhibitors of Methionine AminopeptidasesPyridinylpyrimidines selectively inhibit human methionine aminopeptidase-1Pyridinylquinazolines 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 complexesDiscovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterizationAmino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo.Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediatesExpression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1aAdvances in Bacterial Methionine Aminopeptidase InhibitionChemical shift assignments of zinc finger domain of methionine aminopeptidase 1 (MetAP1) from Homo sapiens.Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.The unique functional role of the C-HS hydrogen bond in the substrate specificity and enzyme catalysis of type 1 methionine aminopeptidase.Large-scale identification of essential Salmonella genes by trapping lethal insertions.Development and validation of a whole-cell inhibition assay for bacterial methionine aminopeptidase by surface-enhanced laser desorption ionization-time of flight mass spectrometryInhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity.Analysis of the stoichiometric metal activation of methionine aminopeptidase.Relationship between operon preference and functional properties of persistent genes in bacterial genomesProtein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases.A cell-based assay that targets methionine aminopeptidase in a physiologically relevant environmentChallenges of antibacterial discoveryPeptide deformylase as a target for new generation, broad spectrum antimicrobial agents.Expression and purification of recombinant hemoglobin in Escherichia coli.Posttranslational protein modification in Archaea.Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.Expression of Escherichia coli methionyl-tRNA formyltransferase in Saccharomyces cerevisiae leads to formylation of the cytoplasmic initiator tRNA and possibly to initiation of protein synthesis with formylmethionine.Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity.Control of protein life-span by N-terminal methionine excisionStructural basis of catalysis by monometalated methionine aminopeptidaseTargeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest
P2860
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P2860
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
description
1989 nî lūn-bûn
@nan
1989 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
name
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@ast
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@en
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@nl
type
label
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@ast
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@en
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@nl
prefLabel
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@ast
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@en
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@nl
P2093
P2860
P1476
Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
@en
P2093
P2860
P304
P356
10.1128/JB.171.7.4071-4072.1989
P407
P577
1989-07-01T00:00:00Z