Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
about
An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathwayHuman mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibioticsIdentification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanismsCrystal structure of type II peptide deformylase from Staphylococcus aureusYcf93 (Orf105), a small apicoplast-encoded membrane protein in the relict plastid of the malaria parasite Plasmodium falciparum that is conserved in ApicomplexaPeptide deformylase inhibitors as antibacterial agents: identification of VRC3375, a proline-3-alkylsuccinyl hydroxamate derivative, by using an integrated combinatorial and medicinal chemistry approach.Transcriptional profiling of Actinobacillus pleuropneumoniae under iron-restricted conditions.Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance.Solvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.Comparative in vitro activities of investigational peptide deformylase inhibitor NVP LBM-415 and other agents against human mycoplasmas and ureaplasmas.Resistance of Streptococcus pneumoniae to deformylase inhibitors is due to mutations in defB.N-alkyl urea hydroxamic acids as a new class of peptide deformylase inhibitors with antibacterial activityControl of protein life-span by N-terminal methionine excisionThe crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms.Antimicrobial activities of endophytic fungi isolated from Ophiopogon japonicus (Liliaceae).Metalloprotease inhibitors GM6001 and TAPI-0 inhibit the obligate intracellular human pathogen Chlamydia trachomatis by targeting peptide deformylase of the bacterium.Reducing the fitness cost of antibiotic resistance by amplification of initiator tRNA genes.Overexpression of peptide deformylase in breast, colon, and lung cancers.Novel agents for the treatment of resistant Gram-positive infections.Regulation of gene expression in Streptococcus pneumoniae by response regulator 09 is strain dependentStructure-Based Drug Design of Small Molecule Peptide Deformylase Inhibitors to Treat Cancer.Therapeutic potential of peptide deformylase inhibitors.Relative quantitative comparisons of the extracellular protein profiles of Staphylococcus aureus UAMS-1 and its sarA, agr, and sarA agr regulatory mutants using one-dimensional polyacrylamide gel electrophoresis and nanocapillary liquid chromatograpMutations in three distinct loci cause resistance to peptide deformylase inhibitors in Bacillus subtilis.Formyl peptide receptors are candidate chemosensory receptors in the vomeronasal organ.The Inhibition and Resistance Mechanisms of Actinonin, Isolated from Marine Streptomyces sp. NHF165, against Vibrio anguillarum.In vivo characterization of the peptide deformylase inhibitor LBM415 in murine infection models.A unique peptide deformylase platform to rationally design and challenge novel active compounds.Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery.Novel Helicobacter pylori therapeutic targets: the unusual suspects.Three consecutive arginines are important for the mycobacterial peptide deformylase enzyme activityProteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition.SILProNAQ: A Convenient Approach for Proteome-Wide Analysis of Protein N-Termini and N-Terminal Acetylation Quantitation.Zinc-selective inhibition of the promiscuous bacterial amide-hydrolase DapE: implications of metal heterogeneity for evolution and antibiotic drug design.Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae.Identification of regions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosis.Staphylococcus aureus formyl-methionyl transferase mutants demonstrate reduced virulence factor production and pathogenicityFE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.Proteomic study of peptide deformylase inhibition in Streptococcus pneumoniae and Staphylococcus aureus.Phylogenomic and biochemical characterization of three Legionella pneumophila polypeptide deformylases.
P2860
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P2860
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@ast
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@en
type
label
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@ast
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@en
prefLabel
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@ast
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@en
P2093
P2860
P1476
Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.2000.01908.X
P407
P577
2000-06-01T00:00:00Z