Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27644223

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Magic angle spinning NMR of viruses Recent progress in structure-based anti-influenza drug design M2 protein from influenza A: from multiple structures to biophysical and functional insights NMR structures of membrane proteins in phospholipid bilayers Conformational changes induced by a single amino acid substitution in thetrans-membrane domain of Vpu: Implications for HIV-1 susceptibility to channel blocking drugs 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 Backbone structure of a small helical integral membrane protein: A unique structural characterization Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus 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 Influenza M2 proton channels The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic Resonance NMR structures of polytopic integral membrane proteins.Solid state NMR: The essential technology for helical membrane protein structural characterization.Assignment of oriented sample NMR resonances from a three transmembrane helix protein.Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature.Probing membrane protein structure using water polarization transfer solid-state NMR.Survival analysis of infected mice reveals pathogenic variations in the genome of avian H1N1 viruses A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.Structures of influenza A proteins and insights into antiviral drug targets.Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Membrane protein structure and dynamics from NMR spectroscopy.Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza a M2 protein functional insights.Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.Solid state NMR strategy for characterizing native membrane protein structures Structural basis for proton conduction and inhibition by the influenza M2 protein.Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Solid state NMR and protein-protein interactions in membranes Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Free-energy profiles for ions in the influenza M2-TMD channel Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes.Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.Conformational heterogeneity of the M2 proton channel and a structural model for channel activation

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P2860

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

http://www.wikidata.org/entity/Q27644223

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2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007年の論文

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Backbone Structure of the Aman ...... Channel from Influenza A Virus

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Biophysical Journal

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Backbone Structure of the Aman ...... Channel from Influenza A Virus

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Conggang Li

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Jack R Quine

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Jun Hu

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Richard Bertram

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Riqiang Fu

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Srisairam Achuthan

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Timothy A Cross

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Tom Asbury

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

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

Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms

Structure of the transmembrane region of the M2 protein H+ channel

The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR

A transmembrane helix dimer: structure and implications

The Xplor-NIH NMR molecular structure determination package

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

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

A graph-theory algorithm for rapid protein side-chain prediction

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