Structure and function of the influenza A M2 proton channel
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Viral Membrane Channels: Role and Function in the Virus Life CycleStructural basis for the function and inhibition of an influenza virus proton channelStructure of the amantadine binding site of influenza M2 proton channels in lipid bilayersStructure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virusThe Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic ResonanceStructures of influenza A proteins and insights into antiviral drug targets.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.Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus.Considering protonation as a posttranslational modification regulating protein structure and function.Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shiftsStructural basis for proton conduction and inhibition by the influenza M2 protein.pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMRConformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conductionConformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMRProtonation, tautomerization, and rotameric structure of histidine: a comprehensive study by magic-angle-spinning solid-state NMR.NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibitionProton and cation transport activity of the M2 proton channel from influenza A virus.NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide.Novel antigens for RSV vaccines.Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Exploring Histidine Conformations in the M2 Channel Lumen of the Influenza A Virus at Neutral pH via Molecular SimulationsInfluenza virus A M2 protein generates negative Gaussian membrane curvature necessary for budding and scission.Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Influenza a virus entry: implications in virulence and future therapeutics.Exploring the size limit of templates for inhibitors of the M2 ion channel of influenza A virus.Synthesis and Crystallographic Insight into the Structural Aspects of Some Novel Adamantane-Based Ester Derivatives.Adamantane in Drug Delivery Systems and Surface Recognition.Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes.Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness.The Molecular Switch of Telomere Phages: High Binding Specificity of the PY54 Cro Lytic Repressor to a Single Operator Site.Structural biology. The flu's proton escort.Magic-angle-spinning NMR of the drug resistant S31N M2 proton transporter from influenza A.Modulating secretory pathway pH by proton channel co-expression can increase recombinant protein stability in plants.
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P2860
Structure and function of the influenza A M2 proton channel
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on August 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Structure and function of the influenza A M2 proton channel
@en
Structure and function of the influenza A M2 proton channel.
@nl
type
label
Structure and function of the influenza A M2 proton channel
@en
Structure and function of the influenza A M2 proton channel.
@nl
prefLabel
Structure and function of the influenza A M2 proton channel
@en
Structure and function of the influenza A M2 proton channel.
@nl
P2860
P356
P1433
P1476
Structure and function of the influenza A M2 proton channel
@en
P2093
Fanghao Hu
Wenbin Luo
P2860
P304
P356
10.1021/BI9008837
P407
P577
2009-08-01T00:00:00Z