Structural basis and mechanism of enoyl reductase inhibition by triclosan
about
The evolution, metabolism and functions of the apicoplastStructural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductaseInhibition of the Mycobacterium tuberculosis enoyl acyl carrier protein reductase InhA by arylamidesSlow-Onset Inhibition of the FabI Enoyl Reductase from Francisella tularensis : Residence Time and in Vivo ActivityCrystal Structures of Mycobacterium tuberculosis KasA Show Mode of Action within Cell Wall Biosynthesis and its Inhibition by ThiolactomycinStructure of theFrancisella tularensisenoyl-acyl carrier protein reductase (FabI) in complex with NAD+and triclosanEffect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from Plasmodium falciparumDetermination of the Crystal Structure and Active Residues of FabV, the Enoyl-ACP Reductase from Xanthomonas oryzaeStructure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone InhibitorsStaphylococcus 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) InhibitorsTime-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 InhibitorResistance Mechanisms and the Future of Bacterial Enoyl-Acyl Carrier Protein Reductase (FabI) AntibioticsInhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachloropheneCrystal structure of the human fatty acid synthase enoyl-acyl carrier protein-reductase domain complexed with triclosan reveals allosteric protein-protein interface inhibitionTriclosan Demonstrates Synergic Effect with Amphotericin B and Fluconazole and Induces Apoptosis-Like Cell Death in Cryptococcus neoformansA novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticolaMechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia malleiInhibition of light emission from the bioluminescent bacterium Vibrio fischeri after exposure to triclosan and related hygiene care products.Pyrrolidine carboxamides as a novel class of inhibitors of enoyl acyl carrier protein reductase from Mycobacterium tuberculosisRational Modulation of the Induced-Fit Conformational Change for Slow-Onset Inhibition in Mycobacterium tuberculosis InhA.Drug-target residence time: critical information for lead optimization.Discovery of a novel and potent class of F. tularensis enoyl-reductase (FabI) inhibitors by molecular shape and electrostatic matchingMutational analysis of the triclosan-binding region of enoyl-ACP (acyl-carrier protein) reductase from Plasmodium falciparum.Mechanism and inhibition of the FabI enoyl-ACP reductase from Burkholderia pseudomalleiBacterial target sites for biocide action.Mechanisms of bacterial biocide and antibiotic resistance.Potential impact of increased use of biocides in consumer products on prevalence of antibiotic resistanceComputational conformational antimicrobial analysis developing mechanomolecular theory for polymer biomaterials in materials science and engineering.Triclosan Computational Conformational Chemistry Analysis for Antimicrobial Properties in PolymersAnalysis of Enoyl-Acyl Carrier Protein Reductase Structure and Interactions Yields an Efficient Virtual Screening Approach and Suggests a Potential Allosteric Site.Radiolabelling and positron emission tomography of PT70, a time-dependent inhibitor of InhA, the Mycobacterium tuberculosis enoyl-ACP reductase.Aqueous Molecular Dynamics Simulations of the M. tuberculosis Enoyl-ACP Reductase-NADH System and Its Complex with a Substrate Mimic or Diphenyl Ethers Inhibitors.Crystallographic insights into the structure-activity relationships of diazaborine enoyl-ACP reductase inhibitors.Inhibiting bacterial fatty acid synthesis.New developments in ureteral stent design, materials and coatings.The Francisella tularensis FabI enoyl-acyl carrier protein reductase gene is essential to bacterial viability and is expressed during infection.Strategies for the development of the urinary catheter.Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli
P2860
Q24652914-65489F10-5BB5-4EB9-B5AB-BD9524636152Q27637344-95192318-CF74-4D63-88D3-B1C6029E92E8Q27647576-6BBB8828-3C2A-4827-A3D1-D6143A0D990EQ27653711-1C4A6D0F-3439-48A2-88F3-ED51AC678CBFQ27656454-591FCB39-4581-42F6-8D07-A479363E56F7Q27665567-6B33891A-0A7F-400D-8889-D37131676C70Q27666619-0C0EABB0-0559-4E84-9F16-34A8B3A9C196Q27675305-9DE6D897-8F85-4AD4-9D30-441B0E09A535Q27676726-AFB9C0BA-AF54-4641-9AAA-C588D8D4C976Q27679034-8A14B998-1E78-4290-BBF1-BA0974BF645EQ27679331-BBA795F4-1D7B-4EA1-A205-FC7D257B151EQ27682088-35295EBD-7C78-4304-AB6D-95EBFB07E892Q27683440-142750BE-6AC9-4B41-AC9D-2F35B49CD662Q28069943-F12B1F18-BE0C-409E-9698-AA6E1D99DF02Q28370360-1B503A96-8CF2-45E4-9D76-DB1144B9B2C1Q28383149-8356FB89-3B3F-47DF-B242-A3BF570B2FC9Q28390076-82BA7D76-AF56-49EF-BD97-1F12637E7F64Q28485601-585C7EC1-6EAD-4401-88AD-775C52793796Q28492113-6969001E-25D4-4F94-9785-F028C985CD40Q31950273-5137E27B-143C-4B46-AF02-1DCF21AAD322Q33260049-AC4E83BA-03B6-4800-B629-69C49C0872CCQ34044404-15D7D51E-6E1C-4EA9-8F72-59E62B7DB95AQ34054343-F1543F3D-7840-4D2B-8767-A965C9548CE0Q34078440-40528B69-3CC3-40C0-BFE0-FAA2AC16164CQ34320334-4AB4F2E8-F366-4A10-BD59-F418E0FEBE95Q34566539-050130F3-8149-4061-8AD8-006EE4ECECA8Q34631424-F0E71D70-F409-4CAA-BF5C-65B2061CA17EQ34631438-2389CDE3-252C-4FC6-930B-84AC4C0F37BDQ34927172-B3F948D6-FE4B-4B2B-99B0-4C2A6AE27819Q34971535-19306F76-395C-4168-9F79-0532A3F7A340Q35383118-0B580500-980C-4C92-903B-B10A8E768092Q35741705-5B6B20B0-75D3-4370-862A-6F3D35872955Q36167169-BDF597A1-7488-485A-A7FA-3F51F2DE86D4Q36247329-067EE351-E451-4685-AF03-C4E685ED1409Q36337901-243E5C7B-2EFF-47EC-B9EB-164E394EF97BQ36464020-7674B85D-0679-4E19-AC8F-E7EF47FFEA75Q36471570-7198A3D6-ABB3-4A0A-BD94-ECB2217530AAQ36558861-A1ECF471-C7E8-4FB5-B680-6AA40239DF33Q36759523-6F2A5ED2-9768-41D9-91FC-9D33F5798E92Q36760116-C650675A-F0CA-4DF7-BF38-19020383304A
P2860
Structural basis and mechanism of enoyl reductase inhibition by triclosan
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@ast
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@en
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@nl
type
label
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@ast
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@en
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@nl
prefLabel
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@ast
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@en
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@nl
P2093
P3181
P356
P1476
Structural basis and mechanism of enoyl reductase inhibition by triclosan
@en
P2093
P304
P3181
P356
10.1006/JMBI.1999.2907
P407
P577
1999-07-01T00:00:00Z