Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir - Wikidata - awgldk - TriplyDB

Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir

Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir

http://www.wikidata.org/entity/Q27643632

about

Darunavir, a conceptually new HIV-1 protease inhibitor for the treatment of drug-resistant HIV Rational approaches to improving selectivity in drug design Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir 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 ∞Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters Probing Multidrug-Resistance and Protein-Ligand Interactions with Oxatricyclic Designed Ligands in HIV-1 Protease Inhibitors The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts Novel P2 Tris-tetrahydrofuran Group in Antiviral Compound 1 (GRL-0519) Fills the S2 Binding Pocket of Selected Mutants of HIV-1 Protease Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors Terminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 Protease 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 Carbamylation of N-Terminal Proline Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics Sparse Representation for Prediction of HIV-1 Protease Drug Resistance.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.Capturing the essence of organic synthesis: from bioactive natural products to designed molecules in today's medicine.Defective hydrophobic sliding mechanism and active site expansion in HIV-1 protease drug resistant variant Gly48Thr/Leu89Met: mechanisms for the loss of saquinavir binding potency Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism.Virtual Screening of Indonesian Herbal Database as HIV-1 Protease Inhibitor.HIV-1 Protease: Structural Perspectives on Drug Resistance Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism Active-site mutations in the South african human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study.Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors.Testing the substrate-envelope hypothesis with designed pairs of compounds.Enhancing protein backbone binding--a fruitful concept for combating drug-resistant HIV.Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS Ramachandran analysis of conserved glycyl residues in homologous proteins of known structure Combating HIV resistance - focus on darunavir.Insight into the structural similarity between HIV protease and secreted aspartic protease-2 and binding mode analysis of HIV-Candida albicans inhibitors.Fast and accurate determination of the relative binding affinities of small compounds to HIV-1 protease using non-equilibrium work.

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P2860

Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir

http://www.wikidata.org/entity/Q27643632

description

2007 nî lūn-bûn

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2007 թվականի ապրիլին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Atomic resolution crystal stru ...... V82A and I84V with saquinavir

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Andrey Y Kovalevsky

http://www.w3.org/2001/XMLSchema#string

Arun K Ghosh

http://www.w3.org/2001/XMLSchema#string

Irene T Weber

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Peter Boross

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Robert W Harrison

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Yuan-Fang Wang

http://www.w3.org/2001/XMLSchema#string

Yunfeng Tie

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P2860

In vivo resistance to a human immunodeficiency virus type 1 proteinase inhibitor: mutations, kinetics, and frequencies.

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232-42

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scholarly article

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4051343

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10.1002/PROT.21304

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1

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67

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crystal structure