Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV ProteaseDrug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 ProteaseThermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteasesInference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 Protease.Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 proteaseDefective hydrophobic sliding mechanism and active site expansion in HIV-1 protease drug resistant variant Gly48Thr/Leu89Met: mechanisms for the loss of saquinavir binding potencyEffects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.Modulation of HIV protease flexibility by the T80N mutationIdentifying binding hot spots on protein surfaces by mixed-solvent molecular dynamics: HIV-1 protease as a test caseAnalysis of the Zidovudine Resistance Mutations T215Y, M41L, and L210W in HIV-1 Reverse Transcriptase.Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.Improving Viral Protease Inhibitors to Counter Drug Resistance.Rigidity versus flexibility: the dilemma of understanding protein thermal stability.Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.Comparison of the molecular dynamics and calculated binding free energies for nine FDA-approved HIV-1 PR drugs against subtype B and C-SA HIV PR.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.Multi-drug resistance profile of PR20 HIV-1 protease is attributed to distorted conformational and drug binding landscape: molecular dynamics insights.Amide hydrogen exchange in HIV-1 subtype B and C proteases--insights into reduced drug susceptibility and dimer stability.Drug-resistant HIV-1 protease regains functional dynamics through cleavage site coevolution.Uniquely localized intra-molecular amino acid concentrations at the glycolytic enzyme catalytic/active centers of Archaea, Bacteria and Eukaryota are associated with their proposed temporal appearances on earth.Binding Free Energy Calculations of Nine FDA-approved Protease Inhibitors Against HIV-1 Subtype C I36T↑T Containing 100 Amino Acids Per Monomer.Interchain hydrophobic clustering promotes rigidity in HIV-1 protease flap dynamics: new insights from molecular dynamics.Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases.
P2860
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P2860
Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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2012 թուականի Մարտին հրատարակուած գիտական յօդուած
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2012 թվականի մարտին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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name
Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
@ast
Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
@en
Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
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P2093
P2860
P356
P1476
Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
@en
P2093
Celia A Schiffer
Madhavi N L Nalam
Seema Mittal
Yufeng Cai
P2860
P304
P356
10.1021/JA2095766
P407
P50
P577
2012-03-07T00:00:00Z