Evaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed To Be Robust against Drug Resistance - Wikidata - thesis-toulmin - TriplyDB

Evaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed To Be Robust against Drug Resistance

Evaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed To Be Robust against Drug Resistance

http://www.wikidata.org/entity/Q27660267

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Structure-based methods for predicting target mutation-induced drug resistance and rational drug design to overcome the problem Rational approaches to improving selectivity in drug design A virtual screen discovers novel, fragment-sized inhibitors of Mycobacterium tuberculosis InhA Design of a Potent D-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to Resistance Structure-Based Design, Synthesis, and Structure−Activity Relationship Studies of HIV-1 Protease Inhibitors Incorporating Phenyloxazolidinones Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding Nine crystal structures determine the substrate envelope of the MDR HIV-1 protease Molecular Mechanisms of Viral and Host Cell Substrate Recognition by Hepatitis C Virus NS3/4A Protease The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors Molecular Mechanism by Which a Potent Hepatitis C Virus NS3-NS4A Protease Inhibitor Overcomes Emergence of Resistance Structural and Thermodynamic Basis of Amprenavir/Darunavir and Atazanavir Resistance in HIV-1 Protease with Mutations at Residue 50 Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV Protease Substrate Envelope-Designed Potent HIV-1 Protease Inhibitors to Avoid Drug Resistance Design, Synthesis, and Biological and Structural Evaluations of Novel HIV-1 Protease Inhibitors To Combat Drug Resistance Drug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 Protease Structural and Thermodynamic Effects of Macrocyclization in HCV NS3/4A Inhibitor MK-5172 Characterization of small molecule binding. I. Accurate identification of strong inhibitors in virtual screening Efficient Computation of Small-Molecule Configurational Binding Entropy and Free Energy Changes by Ensemble Enumeration MCPath: Monte Carlo path generation approach to predict likely allosteric pathways and functional residues.Higher Desolvation Energy Reduces Molecular Recognition in Multi-Drug Resistant HIV-1 Protease VASP: a volumetric analysis of surface properties yields insights into protein-ligand binding specificity.Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism.Molecular Basis for Drug Resistance in HIV-1 Protease Protocol for rational design of covalently interacting inhibitors.Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.Interaction of I50V mutant and I50L/A71V double mutant HIV-protease with inhibitor TMC114 (darunavir): molecular dynamics simulation and binding free energy studies.Modeling Protein-Ligand Binding by Mining Minima.Interdependence of Inhibitor Recognition in HIV-1 Protease.The structural biology of HIV-1: mechanistic and therapeutic insights Molecular mechanisms and design principles for promiscuous inhibitors to avoid drug resistance: lessons learned from HIV-1 protease inhibition.Improving Viral Protease Inhibitors to Counter Drug Resistance.Testing the substrate-envelope hypothesis with designed pairs of compounds.Improving the Resistance Profile of Hepatitis C NS3/4A Inhibitors: Dynamic Substrate Envelope Guided Design Effect of polarization on HIV-1protease and fluoro-substituted inhibitors binding energies by large scale molecular dynamics simulations.Human Immunodeficiency Virus Gag and protease: partners in resistance.Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS Molecular and Dynamic Mechanism Underlying Drug Resistance in Genotype 3 Hepatitis C NS3/4A Protease.Elucidating the Interdependence of Drug Resistance from Combinations of Mutations.Discovery of Novel Peptidomimetics as Irreversible CHIKV NsP2 Protease Inhibitors Using Quantum Mechanical-Based Ligand Descriptors.A combined 3D-QSAR and docking studies for the In-silico prediction of HIV-protease inhibitors.

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Evaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed To Be Robust against Drug Resistance

http://www.wikidata.org/entity/Q27660267

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2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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Evaluating the Substrate-Envel ...... Robust against Drug Resistance

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Evaluating the Substrate-Envel ...... Robust against Drug Resistance

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Evaluating the Substrate-Envel ...... Robust against Drug Resistance

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Evaluating the Substrate-Envel ...... Robust against Drug Resistance

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Evaluating the substrate-envel ...... robust against drug resistance

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Akbar Ali

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Celia A Schiffer

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G S Kiran Kumar Reddy

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Hong Cao

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Madhavi N L Nalam

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Michael D Altman

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Michael K Gilson

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Sripriya Chellappan

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Tariq M Rana

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P2860

Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes

Discovery of HIV-1 protease inhibitors with picomolar affinities incorporating N-aryl-oxazolidinone-5-carboxamides as novel P2 ligands

Design of mutation-resistant HIV protease inhibitors with the substrate envelope hypothesis

HIV-1 Protease Inhibitors from Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant Variants

ABT-538 is a potent inhibitor of human immunodeficiency virus protease and has high oral bioavailability in humans

Viracept (nelfinavir mesylate, AG1343): a potent, orally bioavailable inhibitor of HIV-1 protease

Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer

Rational design of peptide-based HIV proteinase inhibitors

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ABT-378, a highly potent inhibitor of the human immunodeficiency virus protease

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10.1128/JVI.02531-09

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10

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20237088

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