Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality - Test2 - elhamkhani - TriplyDB

Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality

Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality

http://www.wikidata.org/entity/Q27679034

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An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.Mode of Action, In Vitro Activity, and In Vivo Efficacy of AFN-1252, a Selective Antistaphylococcal FabI Inhibitor Rational Optimization of Drug-Target Residence Time: Insights from Inhibitor Binding to the Staphylococcus aureus FabI Enzyme–Product Complex Structural Basis for the Recognition of Mycolic Acid Precursors by KasA, a Condensing Enzyme and Drug Target from Mycobacterium Tuberculosis Crystal structures and kinetic properties of enoyl-acyl carrier protein reductase I fromCandidatus Liberibacter asiaticus A structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.Rational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (ACP) Reductase Inhibitor Type II Fatty Acid Synthesis Is Essential for the Replication of Chlamydia trachomatis Slow-Onset Inhibition of Mycobacterium tuberculosis InhA: Revealing Molecular Determinants of Residence Time by MD Simulations Do Halogen-Hydrogen Bond Donor Interactions Dominate the Favorable Contribution of Halogens to Ligand-Protein Binding?Staphylococcus aureus but not Listeria monocytogenes adapt to triclosan and adaptation correlates with increased fabI expression and agr deficiency Analysis of Enoyl-Acyl Carrier Protein Reductase Structure and Interactions Yields an Efficient Virtual Screening Approach and Suggests a Potential Allosteric Site.The Francisella tularensis FabI enoyl-acyl carrier protein reductase gene is essential to bacterial viability and is expressed during infection.Efficacy and Safety of AFN-1252, the First Staphylococcus-Specific Antibacterial Agent, in the Treatment of Acute Bacterial Skin and Skin Structure Infections, Including Those in Patients with Significant Comorbidities Selectivity of Pyridone- and Diphenyl Ether-Based Inhibitors for the Yersinia pestis FabV Enoyl-ACP Reductase.Insights into the Mechanism of Homeoviscous Adaptation to Low Temperature in Branched-Chain Fatty Acid-Containing Bacteria through Modeling FabH Kinetics from the Foodborne Pathogen Listeria monocytogenes.Comparative Proteomic Analysis of Differential Proteins in Response to Aqueous Extract of Quercus infectoria Gall in Methicillin-Resistant Staphylococcus aureus.Environmental fatty acids enable emergence of infectious Staphylococcus aureus resistant to FASII-targeted antimicrobials.Resistance to AFN-1252 arises from missense mutations in Staphylococcus aureus enoyl-acyl carrier protein reductase (FabI).Safety, tolerability and pharmacokinetics of AFN-1252 administered as immediate release tablets in healthy subjects.Recent Advances in the Rational Design and Optimization of Antibacterial Agents.Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.Clinical Relevance of Type II Fatty Acid Synthesis Bypass in Staphylococcus aureus.Correlating Drug-Target Kinetics and In vivo Pharmacodynamics: Long Residence Time Inhibitors of the FabI Enoyl-ACP Reductase.Characterization of FabG and FabI of the Streptomyces coelicolor dissociated fatty acid synthase.Parametrization of halogen bonds in the CHARMM general force field: Improved treatment of ligand-protein interactions.A [(32)P]NAD(+)-based method to identify and quantitate long residence time enoyl-acyl carrier protein reductase inhibitors An Efficient and Economical Assay to Screen for Triclosan Binding to FabI.

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Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality

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2012 nî lūn-bûn

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2012年の論文

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Staphylococcus aureus FabI: In ...... tions for In Vivo Essentiality

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THE STRUCTURAL BIOLOGY OF TYPE II FATTY ACID BIOSYNTHESIS

Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus

Basic local alignment search tool

Structural basis and mechanism of enoyl reductase inhibition by triclosan

The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family

Design and Synthesis of Aryl Ether Inhibitors of theBacillus AnthracisEnoyl-ACP Reductase

Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella tularensis : Residence Time and in Vivo Activity

Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP and triclosan

Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus

Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis

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224948509

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22579249

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structural biology

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