Inhibitors of FabI, an enzyme drug target in the bacterial fatty acid biosynthesis pathway.
about
Investigational drugs to treat methicillin-resistant Staphylococcus aureusBacterial lipids: metabolism and membrane homeostasisA virtual screen discovers novel, fragment-sized inhibitors of Mycobacterium tuberculosis InhADesign and Synthesis of Aryl Ether Inhibitors of theBacillus AnthracisEnoyl-ACP ReductaseSlow-Onset Inhibition of the FabI Enoyl Reductase from Francisella tularensis : Residence Time and in Vivo ActivityA Slow, Tight Binding Inhibitor of InhA, the Enoyl-Acyl Carrier Protein Reductase from Mycobacterium tuberculosisStructure of theFrancisella tularensisenoyl-acyl carrier protein reductase (FabI) in complex with NAD+and triclosanMode of Action, In Vitro Activity, and In Vivo Efficacy of AFN-1252, a Selective Antistaphylococcal FabI InhibitorTowards a new tuberculosis drug: pyridomycin - nature's isoniazidStructure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone InhibitorsRational Optimization of Drug-Target Residence Time: Insights from Inhibitor Binding to the Staphylococcus aureus FabI Enzyme–Product ComplexStaphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo EssentialityStructural and Enzymatic Analyses Reveal the Binding Mode of a Novel Series of Francisella tularensis Enoyl Reductase (FabI) InhibitorsA structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.Time-Dependent Diaryl Ether Inhibitors of InhA: Structure-Activity Relationship Studies of Enzyme Inhibition, Antibacterial Activity, and in vivo EfficacyRational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (ACP) Reductase InhibitorStructural and biochemical characterization of an atypical short-chain dehydrogenase/reductase reveals an unusual cofactor preferenceDrug discovery using chemical systems biology: repositioning the safe medicine Comtan to treat multi-drug and extensively drug resistant tuberculosisThe Mycobacterium tuberculosis drugome and its polypharmacological implicationsMechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia malleiAntibiotics in the clinical pipeline at the end of 2015.Dynamics of Plasmodium falciparum enoyl-ACP reductase and implications on drug discovery.Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin.Challenges of antibacterial discoveryUnderstanding ligand-receptor non-covalent binding kinetics using molecular modeling.Targeting tuberculosis through a small focused library of 1,2,3-triazoles.Experimental annotation of post-translational features and translated coding regions in the pathogen Salmonella TyphimuriumDrug-target residence time: critical information for lead optimization.1,4-azaindole, a potential drug candidate for treatment of tuberculosis.Discovery of a novel and potent class of F. tularensis enoyl-reductase (FabI) inhibitors by molecular shape and electrostatic matchingMechanisms of self-resistance in the platensimycin- and platencin-producing Streptomyces platensis MA7327 and MA7339 strains.Mechanism and inhibition of the FabI enoyl-ACP reductase from Burkholderia pseudomalleiRadiosynthesis and biological evaluation of a novel enoyl-ACP reductase inhibitor for Staphylococcus aureusComplexomics study of two Helicobacter pylori strains of two pathological origins: potential targets for vaccine development and new insight in bacteria metabolism.Meleagrin, a new FabI inhibitor from Penicillium chryosogenum with at least one additional mode of action.Metabolic basis for the differential susceptibility of Gram-positive pathogens to fatty acid synthesis inhibitors.The MUT056399 inhibitor of FabI is a new antistaphylococcal compound.Is bacterial fatty acid synthesis a valid target for antibacterial drug discovery?Discovery of novel bacterial elongation condensing enzyme inhibitors by virtual screening.Analysis of Enoyl-Acyl Carrier Protein Reductase Structure and Interactions Yields an Efficient Virtual Screening Approach and Suggests a Potential Allosteric Site.
P2860
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P2860
Inhibitors of FabI, an enzyme drug target in the bacterial fatty acid biosynthesis pathway.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@ast
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@en
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@nl
type
label
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@ast
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@en
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@nl
prefLabel
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@ast
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@en
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@nl
P356
P1476
Inhibitors of FabI, an enzyme ...... tty acid biosynthesis pathway.
@en
P2093
P356
10.1021/AR700156E
P407
P577
2008-01-01T00:00:00Z