Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance.
about
New antibiotic molecules: bypassing the membrane barrier of gram negative bacteria increases the activity of peptide deformylase inhibitorsFmt bypass in Pseudomonas aeruginosa causes induction of MexXY efflux pump expressionReduced susceptibility of Haemophilus influenzae to the peptide deformylase inhibitor LBM415 can result from target protein overexpression due to amplified chromosomal def gene copy number.Antibiotics and bacterial resistance in the 21st century.The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms.Dysregulation of bacterial proteolytic machinery by a new class of antibiotics.Therapeutic potential of peptide deformylase inhibitors.Drug forecast - the peptide deformylase inhibitors as antibacterial agents.In vivo characterization of the peptide deformylase inhibitor LBM415 in murine infection models.Potent sub-MIC effect of GSK1322322 and other peptide deformylase inhibitors on in vitro growth of Staphylococcus aureus.Novel Helicobacter pylori therapeutic targets: the unusual suspects.Comparative analysis of the antibacterial activity of a novel peptide deformylase inhibitor, GSK1322322.Pharmacokinetics/Pharmacodynamics of Peptide Deformylase Inhibitor GSK1322322 against Streptococcus pneumoniae, Haemophilus influenzae, and Staphylococcus aureus in Rodent Models of Infection.Frequency of Spontaneous Resistance to Peptide Deformylase Inhibitor GSK1322322 in Haemophilus influenzae, Staphylococcus aureus, Streptococcus pyogenes, and Streptococcus pneumoniae.Activity of LBM415 compared to those of 11 other agents against Haemophilus species.Role of the AcrAB-TolC efflux pump in determining susceptibility of Haemophilus influenzae to the novel peptide deformylase inhibitor LBM415.Multistep resistance selection and postantibiotic-effect studies of the antipneumococcal activity of LBM415 compared to other agentsProteomic study of peptide deformylase inhibition in Streptococcus pneumoniae and Staphylococcus aureus.Phylogenomic and biochemical characterization of three Legionella pneumophila polypeptide deformylases.Virtual Screening Approach of Bacterial Peptide Deformylase Inhibitors Results in New Antibiotics.Pharmacokinetics and unexpected safety issues of LBM415, a novel oral peptide deformylase inhibitor.
P2860
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P2860
Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance.
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Comparative antimicrobial char ...... ibitor of clinical importance.
@ast
Comparative antimicrobial char ...... ibitor of clinical importance.
@en
type
label
Comparative antimicrobial char ...... ibitor of clinical importance.
@ast
Comparative antimicrobial char ...... ibitor of clinical importance.
@en
prefLabel
Comparative antimicrobial char ...... ibitor of clinical importance.
@ast
Comparative antimicrobial char ...... ibitor of clinical importance.
@en
P2093
P2860
P1476
Comparative antimicrobial char ...... ibitor of clinical importance.
@en
P2093
Ronald N Jones
Roy Cleeland
Thomas R Fritsche
P2860
P304
P356
10.1128/AAC.49.4.1468-1476.2005
P407
P577
2005-04-01T00:00:00Z