Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 Protease
about
Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 proteaseAmprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clustersAutocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistanceThe L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic ContactsTerminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseHIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural RearrangementsHIV-1 Protease-Substrate Coevolution in Nelfinavir ResistanceStructures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open FlapsEffects of Hinge Region Natural Polymorphisms on Human Immunodeficiency Virus-1 Protease Structure, Dynamics and Drug-Pressure EvolutionThe role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamicsPressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach.Understanding HIV-1 protease autoprocessing for novel therapeutic development.Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 proteaseDimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.Computational analysis of HIV-1 protease protein binding pockets.Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 proteaseConformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solutionInhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.HIV-1 Protease: Structural Perspectives on Drug ResistanceImproving the description of salt bridge strength and geometry in a Generalized Born model.Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Conformational variation of an extreme drug resistant mutant of HIV protease.Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 ProteaseARTSY-J: Convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra.Modulation of human immunodeficiency virus type 1 protease autoprocessing by charge properties of surface residue 69.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.Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.Correlating conformational shift induction with altered inhibitor potency in a multidrug resistant HIV-1 protease variant.Cysteine 95 and other residues influence the regulatory effects of Histidine 69 mutations on Human Immunodeficiency Virus Type 1 protease autoprocessing.Improved darunavir genotypic mutation score predicting treatment response for patients infected with HIV-1 subtype B and non-subtype B receiving a salvage regimen.Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.The maturation of HIV-1 protease precursor studied by discrete molecular dynamics.HIV-1 Protease and Substrate Coevolution Validates the Substrate Envelope As the Substrate Recognition Pattern.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.Inhibitor-induced conformational shifts and ligand-exchange dynamics for HIV-1 protease measured by pulsed EPR and NMR spectroscopy.GRL-079, a novel P2-Tp-THF-C5-alkylamine- and P2' -Abt-containing HIV-1 protease inhibitor, is extremely potent against multi-drug-resistant HIV-1 variants including HIVDRVRp51 and has a high genetic barrier against the emergence of resistant varianThermodynamics of strongly allosteric inhibition: a model study of HIV-1 protease
P2860
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P2860
Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 Protease
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@ast
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@en
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@nl
type
label
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@ast
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@en
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@nl
prefLabel
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@ast
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@en
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@nl
P2093
P2860
P356
P1476
Effect of the Active Site D25N ...... g of the Mature HIV-1 Protease
@en
P2093
Fengling Liu
Irene T Weber
Jane M Sayer
John M Louis
Rieko Ishima
P2860
P304
P356
10.1074/JBC.M708506200
P407
P577
2008-05-09T00:00:00Z