Conformational adaptation in drug-target interactions and residence time. - Wikidata - wikimedia - TriplyDB

Conformational adaptation in drug-target interactions and residence time.

Conformational adaptation in drug-target interactions and residence time.

http://www.wikidata.org/entity/Q39711928

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Insights into the inhibition of the p90 ribosomal S6 kinase (RSK) by the flavonol glycoside SL0101 from the 1.5 Å crystal structure of the N-terminal domain of RSK2 with bound inhibitor.Rational Optimization of Drug-Target Residence Time: Insights from Inhibitor Binding to the Staphylococcus aureus FabI Enzyme–Product Complex A structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-ACP reductase InhA.Conformational adaptation drives potent, selective and durable inhibition of the human protein methyltransferase DOT1L Kinetic analysis of drug-protein interactions by affinity chromatography Towards structural systems pharmacology to study complex diseases and personalized medicine The use of thermodynamic and kinetic data in drug discovery: decisive insight or increasing the puzzlement?Time-resolved crystallography using the Hadamard transform RaTrav: a tool for calculating mean first-passage times on biochemical networks.Molecular features of interaction between VEGFA and anti-angiogenic drugs used in retinal diseases: a computational approach Definition of the binding mode of a new class of phosphoinositide 3-kinase α-selective inhibitors using in vitro mutagenesis of non-conserved amino acids and kinetic analysis.Slow inhibition and conformation selective properties of extracellular signal-regulated kinase 1 and 2 inhibitors Radioligand dissociation measurements: potential interference of rebinding and allosteric mechanisms and physiological relevance of the biological model systems.Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics.Exploring avidity: understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands.Drug-target residence time--a case for G protein-coupled receptors.Ligand-detected relaxation dispersion NMR spectroscopy: dynamics of preQ1-RNA binding.The impact of binding thermodynamics on medicinal chemistry optimizations.On the 'micro'-pharmacodynamic and pharmacokinetic mechanisms that contribute to long-lasting drug action.Flexible receptor docking for drug discovery.The drug-target residence time model: a 10-year retrospective.On the different experimental manifestations of two-state 'induced-fit' binding of drugs to their cellular targets Drug-target interaction kinetics: underutilized in drug optimization?Advanced molecular dynamics simulation methods for kinase drug discovery.TSPO ligand residence time: a new parameter to predict compound neurosteroidogenic efficacy.Cell membranes… and how long drugs may exert beneficial pharmacological activity in vivo Conformational energy range of ligands in protein crystal structures: The difficult quest for accurate understanding.Cathepsin B Inhibitors: Combining Dipeptide Nitriles with an Occluding Loop Recognition Element by Click Chemistry.High performance enzyme kinetics of turnover, activation and inhibition for translational drug discovery.Evolution and intelligent design in drug development.Resistance mechanism to an uncompetitive inhibitor of a single-substrate, single-product enzyme: a study of Helicobacter pylori glutamate racemase.Drug-Target Kinetics in Drug Discovery.Discovery of novel insulin-like growth factor-1 receptor inhibitors with unique time-dependent binding kinetics.'Partial' competition of heterobivalent ligand binding may be mistaken for allosteric interactions: a comparison of different target interaction models.Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.Discrimination between conformational selection and induced fit protein-ligand binding using Integrated Global Fit analysis.Correlating Drug-Target Kinetics and In vivo Pharmacodynamics: Long Residence Time Inhibitors of the FabI Enoyl-ACP Reductase.Toward High-Throughput Predictive Modeling of Protein Binding/Unbinding Kinetics.An explicit-solvent conformation search method using open software.How and when does an anticancer drug leave its binding site?

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P2860

Conformational adaptation in drug-target interactions and residence time.

http://www.wikidata.org/entity/Q39711928

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2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

Conformational adaptation in drug-target interactions and residence time.

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Conformational adaptation in drug-target interactions and residence time.

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Conformational adaptation in drug-target interactions and residence time.

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Conformational adaptation in drug-target interactions and residence time.

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Conformational adaptation in drug-target interactions and residence time.

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Conformational adaptation in drug-target interactions and residence time.

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Future Medicinal Chemistry

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Conformational adaptation in drug-target interactions and residence time.

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A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

Ligand binding assays at equilibrium: validation and interpretation

The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance

Preclinical profile of VX-950, a potent, selective, and orally bioavailable inhibitor of hepatitis C virus NS3-4A serine protease

The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site

Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site

Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition

Induced-fit tightens pleuromutilins binding to ribosomes and remote interactions enable their selectivity

Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection

Dynamics connect substrate recognition to catalysis in protein kinase A

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