Effectiveness of nonpeptide clinical inhibitor TMC-114 on HIV-1 protease with highly drug resistant mutations D30N, I50V, and L90M. - Test2 - elhamkhani - TriplyDB

Effectiveness of nonpeptide clinical inhibitor TMC-114 on HIV-1 protease with highly drug resistant mutations D30N, I50V, and L90M.

Effectiveness of nonpeptide clinical inhibitor TMC-114 on HIV-1 protease with highly drug resistant mutations D30N, I50V, and L90M.

http://www.wikidata.org/entity/Q34462935

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Rational approaches to improving selectivity in drug design Unique Flap Conformation in an HIV-1 Protease with High-Level Darunavir Resistance.Unique Thermodynamic Response of Tipranavir to Human Immunodeficiency Virus Type 1 Protease Drug Resistance Mutations Potent New Antiviral Compound Shows Similar Inhibition and Structural Interactions with Drug Resistant Mutants and Wild Type HIV-1 Protease †Caught in the Act: The 1.5 Å Resolution Crystal Structures of the HIV-1 Protease and the I54V Mutant Reveal a Tetrahedral Reaction Intermediate †Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir Structural Evidence for Effectiveness of Darunavir and Two Related Antiviral Inhibitors against HIV-2 Protease Design of HIV-1 Protease Inhibitors with Pyrrolidinones and Oxazolidinones as Novel P1′-Ligands To Enhance Backbone-Binding Interactions with Protease: Synthesis, Biological Evaluation, and Protein−Ligand X-ray Studies ∞Molecular Characterization of Clinical Isolates of Human Immunodeficiency Virus Resistant to the Protease Inhibitor Darunavir Design, Synthesis, Protein−Ligand X-ray Structure, and Biological Evaluation of a Series of Novel Macrocyclic Human Immunodeficiency Virus-1 Protease Inhibitors to Combat Drug Resistance Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance Probing Multidrug-Resistance and Protein-Ligand Interactions with Oxatricyclic Designed Ligands in HIV-1 Protease Inhibitors Capturing the Reaction Pathway in Near-Atomic-Resolution Crystal Structures of HIV-1 Protease Novel P2 Tris-tetrahydrofuran Group in Antiviral Compound 1 (GRL-0519) Fills the S2 Binding Pocket of Selected Mutants of HIV-1 Protease Extreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1′-Pyrrolidinone or P2-Tris-tetrahydrofuran Potent Antiviral HIV-1 Protease Inhibitor GRL-02031 Adapts to the Structures of Drug Resistant Mutants with Its P1′-Pyrrolidinone Ring HIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural Rearrangements 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 Basis of Why Nelfinavir-Resistant D30N Mutant of HIV-1 Protease Remains Susceptible to Saquinavir Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics Inference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.Prediction of potency of protease inhibitors using free energy simulations with polarizable quantum mechanics-based ligand charges and a hybrid water model.Harnessing nature's insight: design of aspartyl protease inhibitors from treatment of drug-resistant HIV to Alzheimer's disease.Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir.Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism.HIV-1 Protease: Structural Perspectives on Drug Resistance Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114 Interaction of I50V mutant and I50L/A71V double mutant HIV-protease with inhibitor TMC114 (darunavir): molecular dynamics simulation and binding free energy studies.Computational studies of difference in binding modes of peptide and non-peptide inhibitors to MDM2/MDMX based on molecular dynamics simulations.A novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI), GRL-98065, is potent against multiple-PI-resistant human immunodeficiency virus in vitro.idTarget: a web server for identifying protein targets of small chemical molecules with robust scoring functions and a divide-and-conquer docking approach Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism Optimal drug cocktail design: methods for targeting molecular ensembles and insights from theoretical model systems.Molecular mechanisms and design principles for promiscuous inhibitors to avoid drug resistance: lessons learned from HIV-1 protease inhibition.Resilience to resistance of HIV-1 protease inhibitors: profile of darunavir.Hydration water and bulk water in proteins have distinct properties in radial distributions calculated from 105 atomic resolution crystal structures Role of darunavir in the management of HIV infection.

P2860

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P2860

Effectiveness of nonpeptide clinical inhibitor TMC-114 on HIV-1 protease with highly drug resistant mutations D30N, I50V, and L90M.

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2006 nî lūn-bûn

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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... utations D30N, I50V, and L90M.

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Effectiveness of nonpeptide cl ...... mutations D30N, I50V, and L90M

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Fengling Liu

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Crystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: Insights into the mechanisms of drug resistance

Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes

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