A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex. - Wikidata - awgldk - TriplyDB

A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.

A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.

http://www.wikidata.org/entity/Q36572105

about

HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 Protease Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease Fragment-Based Screen against HIV Protease Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV Protease A poke in the eye: inhibiting HIV-1 protease through its flap-recognition pocket HIV-1 protease substrate binding and product release pathways explored with coarse-grained molecular dynamics.Kinetic characterization of the critical step in HIV-1 protease maturation HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations.Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease Mechanism of the Association Pathways for a Pair of Fast and Slow Binding Ligands of HIV-1 Protease.Solution conformation and dynamics of the HIV-1 integrase core domain.Gated binding of ligands to HIV-1 protease: Brownian dynamics simulations in a coarse-grained model.Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease.Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.Intramolecular regulation of the sequence-specific mRNA interferase activity of MazF fused to a MazE fragment with a linker cleavable by specific proteases Enzyme Tunnels and Gates As Relevant Targets in Drug Design.Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts.Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Targeting structural flexibility in HIV-1 protease inhibitor binding.Atomistic simulations of the HIV-1 protease folding inhibition.Gates of enzymes.Resurrection of an Urbilaterian U1A/U2B″/SNF protein Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.Resistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach.Enhanced conformational sampling technique provides an energy landscape view of large-scale protein conformational transitions.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.Hydrophobic sliding: a possible mechanism for drug resistance in human immunodeficiency virus type 1 protease.Inhibitor-induced conformational shifts and ligand-exchange dynamics for HIV-1 protease measured by pulsed EPR and NMR spectroscopy.Sequence, Structural Analysis and Metrics to Define the Unique Dynamic Features of the Flap Regions Among Aspartic Proteases.Dispersed phantom scatterer technique reveals subtle differences in substrate recognition by phospholipase D inactive mutants.Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR.Protein-ligand (un)binding kinetics as a new paradigm for drug discovery at the crossroad between experiments and modelling Drug Resistance Mutation L76V Alters Nonpolar Interactions at the Flap-Core Interface of HIV-1 Protease

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P2860

A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.

http://www.wikidata.org/entity/Q36572105

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

A solution NMR study of the bi ...... -1 protease-substrate complex.

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A solution NMR study of the bi ...... -1 protease-substrate complex.

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type

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A solution NMR study of the bi ...... -1 protease-substrate complex.

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A solution NMR study of the bi ...... -1 protease-substrate complex.

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A solution NMR study of the bi ...... -1 protease-substrate complex.

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A solution NMR study of the bi ...... -1 protease-substrate complex.

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Protein Science

P1476

A solution NMR study of the bi ...... -1 protease-substrate complex.

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Dennis A Torchia

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Etsuko Katoh

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John M Louis

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Rieko Ishima

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Toshimasa Yamazaki

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P2860

How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease

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

Three-dimensional structures of HIV-1 and SIV protease product complexes

Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.

A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium.

Curling of flap tips in HIV-1 protease as a mechanism for substrate entry and tolerance of drug resistance.

Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutants

Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations

Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants of the HIV-1 protease

Retroviral proteinases.

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1376-1385

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scholarly article

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10.1110/PS.0300703

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7

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12

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Angela M Gronenborn

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2003-07-01T00:00:00Z

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6889462

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12824484

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2323926

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