Mechanism of 150-cavity formation in influenza neuraminidase. - Wikidata - awgldk - TriplyDB

Mechanism of 150-cavity formation in influenza neuraminidase.

Mechanism of 150-cavity formation in influenza neuraminidase.

http://www.wikidata.org/entity/Q30404742

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Recent progress in structure-based anti-influenza drug design Molecular dynamics, monte carlo simulations, and langevin dynamics: a computational review Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus H1N1 2009 Pandemic Influenza Virus: Resistance of the I223R Neuraminidase Mutant Explained by Kinetic and Structural Analysis Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding Structural basis for a class of nanomolar influenza A neuraminidase inhibitors Flavin-Dependent Thymidylate Synthase as a Drug Target for Deadly Microbes: Mutational Study and a Strategy for Inhibitor Design Synthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility Drug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 Protease Serendipitous discovery of a potent influenza virus a neuraminidase inhibitor Synthesis, structure and inhibitory activity of a stereoisomer of oseltamivir carboxylate Quantitative predictions of binding free energy changes in drug-resistant influenza neuraminidase Plasticity of 150-loop in influenza neuraminidase explored by Hamiltonian replica exchange molecular dynamics simulations The influence of 150-cavity binders on the dynamics of influenza A neuraminidases as revealed by molecular dynamics simulations and combined clustering Locking the 150-cavity open: in silico design and verification of influenza neuraminidase inhibitors The Mechanism by which 146-N-Glycan Affects the Active Site of Neuraminidase Exploring the chemical space of influenza neuraminidase inhibitors Antiviral susceptibility of highly pathogenic avian influenza A(H5N1) viruses isolated from poultry, Vietnam, 2009-2011.Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.From neuraminidase inhibitors to conjugates: a step towards better anti-influenza drugs?Influenza A(H1N1)pdm09 resistance and cross-decreased susceptibility to oseltamivir and zanamivir antiviral drugs.Variable ligand- and receptor-binding hot spots in key strains of influenza neuraminidase.Outside-binding site mutations modify the active site's shapes in neuraminidase from influenza A H1N1.Recent progress and challenges in the discovery of new neuraminidase inhibitors.Speed of conformational change: comparing explicit and implicit solvent molecular dynamics simulations POVME 2.0: An Enhanced Tool for Determining Pocket Shape and Volume Characteristics A virtual screening approach for identifying plants with anti H5N1 neuraminidase activity.Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers.Influenza neuraminidase.Combining molecular docking and molecular dynamics to predict the binding modes of flavonoid derivatives with the neuraminidase of the 2009 H1N1 influenza A virus Molecular dynamics simulation in virus research.Molecular modeling and lead design of substituted zanamivir derivatives as potent anti-influenza drugs.Multistructural hot spot characterization with FTProd.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.Improving the Efficiency of Free Energy Calculations in the Amber Molecular Dynamics Package.The significance of naturally occurring neuraminidase quasispecies of H5N1 avian influenza virus on resistance to oseltamivir: a point of concern Antiviral activity of (+)-rutamarin against Kaposi's sarcoma-associated herpesvirus by inhibition of the catalytic activity of human topoisomerase II.Variational Implicit Solvation with Poisson-Boltzmann Theory.Fitness costs for Influenza B viruses carrying neuraminidase inhibitor-resistant substitutions: underscoring the importance of E119A and H274Y.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2011年の論文

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Mechanism of 150-cavity formation in influenza neuraminidase.

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Nature Communications

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Mechanism of 150-cavity formation in influenza neuraminidase.

@en

P2093

Lane Votapka

http://www.w3.org/2001/XMLSchema#string

Robert V Swift

http://www.w3.org/2001/XMLSchema#string

Robin M Bush

http://www.w3.org/2001/XMLSchema#string

Rommie E Amaro

http://www.w3.org/2001/XMLSchema#string

Ross C Walker

http://www.w3.org/2001/XMLSchema#string

Wilfred W Li

http://www.w3.org/2001/XMLSchema#string

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The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

MrBayes 3: Bayesian phylogenetic inference under mixed models

Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.

VMD: visual molecular dynamics

jModelTest: phylogenetic model averaging

PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations

Comparison of multiple Amber force fields and development of improved protein backbone parameters

The war against influenza: discovery and development of sialidase inhibitors

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10.1038/NCOMMS1390

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3144582

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