Remarkable loop flexibility in avian influenza N1 and its implications for antiviral drug design.
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Recent progress in structure-based anti-influenza drug designMolecular dynamics simulations suggest that electrostatic funnel directs binding of Tamiflu to influenza N1 neuraminidases.Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virusStructural and Functional Analysis of Laninamivir and its Octanoate Prodrug Reveals Group Specific Mechanisms for Influenza NA InhibitionInduced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor bindingSynthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibilitySerendipitous discovery of a potent influenza virus a neuraminidase inhibitorNew small-molecule drug design strategies for fighting resistant influenza AMolecular modeling of swine influenza A/H1N1, Spanish H1N1, and avian H5N1 flu N1 neuraminidases bound to Tamiflu and RelenzaPlasticity of 150-loop in influenza neuraminidase explored by Hamiltonian replica exchange molecular dynamics simulationsThe influence of 150-cavity binders on the dynamics of influenza A neuraminidases as revealed by molecular dynamics simulations and combined clusteringLocking the 150-cavity open: in silico design and verification of influenza neuraminidase inhibitorsInterface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.From neuraminidase inhibitors to conjugates: a step towards better anti-influenza drugs?Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble.Protein loop modeling using a new hybrid energy function and its application to modeling in inaccurate structural environments.Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase.Characterizing loop dynamics and ligand recognition in human- and avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations.Computational studies of H5N1 influenza virus resistance to oseltamivir.Role of secondary sialic acid binding sites in influenza N1 neuraminidasePotential drug-like inhibitors of Group 1 influenza neuraminidase identified through computer-aided drug design.Molecular dynamics simulation of oseltamivir resistance in neuraminidase of avian influenza H5N1 virus.The binding properties of the H5N1 influenza virus neuraminidase as inferred from molecular modeling.Mechanism of 150-cavity formation in influenza neuraminidase.Molecular-level simulation of pandemic influenza glycoproteins.Progress in structure-based drug design against influenza A virus.Recent advances in neuraminidase inhibitor development as anti-influenza drugs.Variable ligand- and receptor-binding hot spots in key strains of influenza neuraminidase.Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase.Using Selectively Applied Accelerated Molecular Dynamics to Enhance Free Energy Calculations.Emerging methods for ensemble-based virtual screening.Effects of Biomolecular Flexibility on Alchemical Calculations of Absolute Binding Free EnergiesImplicit ligand theory: rigorous binding free energies and thermodynamic expectations from molecular docking.Global and local molecular dynamics of a bacterial carboxylesterase provide insight into its catalytic mechanism.Insights into the activity and specificity of Trypanosoma cruzi trans-sialidase from molecular dynamics simulationsIndependent-Trajectories Thermodynamic-Integration Free-Energy Changes for Biomolecular Systems: Determinants of H5N1 Avian Influenza Virus Neuraminidase Inhibition by Peramivir.Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase.Microsecond Molecular Dynamics Simulations of Influenza Neuraminidase Suggest a Mechanism for the Increased Virulence of Stalk-Deletion Mutants.The significance of naturally occurring neuraminidase quasispecies of H5N1 avian influenza virus on resistance to oseltamivir: a point of concern
P2860
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P2860
Remarkable loop flexibility in avian influenza N1 and its implications for antiviral drug design.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Remarkable loop flexibility in ...... ons for antiviral drug design.
@en
Remarkable loop flexibility in ...... ons for antiviral drug design.
@nl
type
label
Remarkable loop flexibility in ...... ons for antiviral drug design.
@en
Remarkable loop flexibility in ...... ons for antiviral drug design.
@nl
prefLabel
Remarkable loop flexibility in ...... ons for antiviral drug design.
@en
Remarkable loop flexibility in ...... ons for antiviral drug design.
@nl
P2093
P356
P1476
Remarkable loop flexibility in ...... ons for antiviral drug design.
@en
P2093
Arthur J Olson
David D L Minh
Lily S Cheng
Rommie E Amaro
Wilfred W Li
William M Lindstrom
P304
P356
10.1021/JA0723535
P407
P577
2007-06-01T00:00:00Z