Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114 - Wikidata - awgldk - TriplyDB

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114

http://www.wikidata.org/entity/Q35608637

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Darunavir, a conceptually new HIV-1 protease inhibitor for the treatment of drug-resistant HIV Potent New Antiviral Compound Shows Similar Inhibition and Structural Interactions with Drug Resistant Mutants and Wild Type HIV-1 Protease †Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 Protease 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 Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters Design of HIV-1 Protease Inhibitors with C3-Substituted Hexahydrocyclopentafuranyl Urethanes as P2-Ligands: Synthesis, Biological Evaluation, and Protein–Ligand X-ray Crystal Structure 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 Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV Protease Extreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1′-Pyrrolidinone or P2-Tris-tetrahydrofuran Substituent effects on P2-cyclopentyltetrahydrofuranyl urethanes: Design, synthesis, and X-ray studies of potent HIV-1 protease inhibitors HIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural Rearrangements Joint X-ray/Neutron Crystallographic Study of HIV-1 Protease with Clinical Inhibitor Amprenavir: Insights for Drug Design Structures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open Flaps Carbamylation of N-Terminal Proline Thermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteases Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.Using the Tools and Resources of the RCSB Protein Data Bank.Computational analysis of HIV-1 protease protein binding pockets.Design and synthesis of potent HIV-1 protease inhibitors incorporating hexahydrofuropyranol-derived high affinity P(2) ligands: structure-activity studies and biological evaluation.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 Current and Novel Inhibitors of HIV Protease Organic carbamates in drug design and medicinal chemistry Computational studies of difference in binding modes of peptide and non-peptide inhibitors to MDM2/MDMX based on molecular dynamics simulations.phenix.mr_rosetta: molecular replacement and model rebuilding with Phenix and Rosetta.Improved crystallographic models through iterated local density-guided model deformation and reciprocal-space refinement.Discovery of HIV Type 1 Aspartic Protease Hit Compounds through Combined Computational Approaches.In vitro phenotypic susceptibility of human immunodeficiency virus type 2 clinical isolates to protease inhibitors.Selection of drug-resistant feline immunodeficiency virus (FIV) encoding FIV/HIV chimeric protease in the presence of HIV-specific protease inhibitors Design and synthesis of stereochemically defined novel spirocyclic P2-ligands for HIV-1 protease inhibitors Role of darunavir in the management of HIV infection.Enhancing protein backbone binding--a fruitful concept for combating drug-resistant HIV.Disubstituted Bis-THF Moieties as New P2 Ligands in Nonpeptidal HIV-1 Protease Inhibitors.Formation of transient dimers by a retroviral protease.Design and Development of Highly Potent HIV-1 Protease Inhibitors with a Crown-Like Oxotricyclic Core as the P2-Ligand To Combat Multidrug-Resistant HIV Variants.

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P2860

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114

http://www.wikidata.org/entity/Q35608637

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2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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J.JMB.2006.08.007

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Journal of Molecular Biology

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Ultra-high resolution crystal ...... for clinical inhibitor TMC114

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Arun K Ghosh

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Fengling Liu

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Irene T Weber

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John M Louis

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Robert W Harrison

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Sofiya Leshchenko

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P2860

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

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

A graphical user interface to the CCP4 program suite

SHELXL: high-resolution refinement

Further additions to MolScript version 1.4, including reading and contouring of electron-density maps

The CCP4 suite: programs for protein crystallography

Inhibitors of HIV-1 protease: a major success of structure-assisted drug design.

Beta-lactam compounds as apparently uncompetitive inhibitors of HIV-1 protease.

Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.

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

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161-173

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10.1016/J.JMB.2006.08.007

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1

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363

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Andrey Kovalevsky

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6828614

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16962136

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crystal structure

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1781337

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