Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers - Test2 - elhamkhani - TriplyDB

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

http://www.wikidata.org/entity/Q27659500

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Inhibitory effects on HAV IRES-mediated translation and replication by a combination of amantadine and interferon-alpha Relevance of Viroporin Ion Channel Activity on Viral Replication and Pathogenesis Magic angle spinning NMR of viruses Obstructing toxin pathways by targeted pore blockage Recent progress in structure-based anti-influenza drug design M2 protein from influenza A: from multiple structures to biophysical and functional insights Viral Membrane Channels: Role and Function in the Virus Life Cycle NMR structures of membrane proteins in phospholipid bilayers Functional characterization of a melittin analog containing a non-natural tryptophan analog Structural basis for the function and inhibition of an influenza virus proton channel Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer Supramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and Molecular Dynamics Simulations High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus Structure Determination of a Membrane Protein in Proteoliposomes Unusual architecture of the p7 channel from hepatitis C virus Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol Inhibitors of the influenza A virus M2 proton channel discovered using a high-throughput yeast growth restoration assay Inhibition of influenza A virus infection in vitro by peptides designed in silico Coadministration of Hedera helix L. Extract Enabled Mice to Overcome Insufficient Protection against Influenza A/PR/8 Virus Infection under Suboptimal Treatment with Oseltamivir PSIONplus: Accurate Sequence-Based Predictor of Ion Channels and Their Types The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic Resonance Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.Solid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints.Efficient, balanced, transmission line RF circuits by back propagation of common impedance nodes.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.Efficient molecular mechanics simulations of the folding, orientation, and assembly of peptides in lipid bilayers using an implicit atomic solvation model.NMR structures of polytopic integral membrane proteins.Drug resistance in influenza A virus: the epidemiology and management.NMR as a tool to investigate the structure, dynamics and function of membrane proteins.Membrane protein structure determination: back to the membrane.Solid state NMR: The essential technology for helical membrane protein structural characterization.Strength of a bifurcated H bond.

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P2860

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

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2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Structure of the amantadine bi ...... ton channels in lipid bilayers

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Structure of the amantadine bi ...... ton channels in lipid bilayers

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Cinque S Soto

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Klaus Schmidt-Rohr

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William F Degrado

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P2860

Structure and mechanism of the M2 proton channel of influenza A virus

Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel

Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block

Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus

Structural basis for the function and inhibition of an influenza virus proton channel

Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine Binding

The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue

Influenza A virus M2 ion channel protein: a structure-function analysis

pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.

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