Accessory mutations maintain stability in drug-resistant HIV-1 protease.
about
Stability-mediated epistasis constrains the evolution of an influenza proteinCurrent perspectives on HIV-1 antiretroviral drug resistanceThe choreography of HIV-1 proteolytic processing and virion assemblySubstrate Envelope-Designed Potent HIV-1 Protease Inhibitors to Avoid Drug ResistanceEffects 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 dynamicsCorrelated electrostatic mutations provide a reservoir of stability in HIV proteaseA Functional Interplay between Human Immunodeficiency Virus Type 1 Protease Residues 77 and 93 Involved in Differential Regulation of Precursor Autoprocessing and Mature Protease ActivityStrong Selection Significantly Increases Epistatic Interactions in the Long-Term Evolution of a ProteinComposite Sequence-Structure Stability Models as Screening Tools for Identifying Vulnerable Targets for HIV Drug and Vaccine Development.Adaptive evolution by recombination is not associated with increased mutation rates in Maize streak virus.Inference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts.Improving Viral Protease Inhibitors to Counter Drug Resistance.Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.HIV-1 Subtype Diversity and Prevalence of Primary Drug Resistance in a Single-Center Pediatric Cohort in Germany.Identification of drug resistance mutations in HIV from constraints on natural evolution.Elucidating the Interdependence of Drug Resistance from Combinations of Mutations.Adaptive HIV-1 evolutionary trajectories are constrained by protein stability.HIV-1 subtypes and drug resistance profiles in a cohort of heterosexual patients in Istanbul, Turkey.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.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.Effects of PRE and POST therapy drug-pressure selected mutations on HIV-1 protease conformational sampling.Biomolecular coevolution and its applications: Going from structure prediction toward signaling, epistasis, and function.Mechanism of Darunavir (DRV)'s High Genetic Barrier to HIV-1 Resistance: A Key V32I Substitution in Protease Rarely Occurs, but Once It Occurs, It Predisposes HIV-1 To Develop DRV Resistance.Quasispecies and Drug Resistance
P2860
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P2860
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@en
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@nl
type
label
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@en
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@nl
prefLabel
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@en
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
@nl
P2860
P1476
Accessory mutations maintain stability in drug-resistant HIV-1 protease
@en
P2093
Bruce E Torbett
P2860
P304
P356
10.1016/J.JMB.2011.03.038
P407
P50
P577
2011-07-01T00:00:00Z