Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel - Wikidata - awgldk - TriplyDB

Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel

Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel

http://www.wikidata.org/entity/Q37282382

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Influenza virus M2 protein mediates ESCRT-independent membrane scission M2 protein from influenza A: from multiple structures to biophysical and functional insights Viral Membrane Channels: Role and Function in the Virus Life Cycle Structural basis for the function and inhibition of an influenza virus proton channel 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 High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction Philosophy of voltage-gated proton channels 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 Drug resistance in influenza A virus: the epidemiology and management.Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Assembly of the m2 tetramer is strongly modulated by lipid chain length.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.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.pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from 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 conduction Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR Influenza virus m2 ion channel protein is necessary for filamentous virion formation.Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump Coexistence of two adamantane binding sites in the influenza A M2 ion channel.Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition Proton and cation transport activity of the M2 proton channel from influenza A virus.Computational study of drug binding to the membrane-bound tetrameric M2 peptide bundle from influenza A virus Functional reconstitution of influenza A M2(22-62).Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes.Multiple Proton Confinement in the M2 Channel from the Influenza A Virus Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channel Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Viral miniproteins Influence of solubilizing environments on membrane protein structures A pH-dependent conformational ensemble mediates proton transport through the influenza A/M2 protein Hydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.De novo design of a transmembrane Zn²⁺-transporting four-helix bundle.

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Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel

http://www.wikidata.org/entity/Q37282382

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 09 July 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

Identification of the function ...... 2 proton-selective ion channel

@en

Identification of the function ...... proton-selective ion channel.

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type

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Identification of the function ...... 2 proton-selective ion channel

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Identification of the function ...... proton-selective ion channel.

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Identification of the function ...... 2 proton-selective ion channel

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Identification of the function ...... proton-selective ion channel.

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PNAS.0905726106

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Proceedings of the National Academy of Sciences of the United States of America

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Identification of the function ...... 2 proton-selective ion channel

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Alexei L Polishchuk

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Amanda L Stouffer

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Arne Schön

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Chunlong Ma

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Emma Magavern

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Ernesto Freire

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James D Lear

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Lawrence H Pinto

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Robert A Lamb

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Xianghong Jing

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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

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

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

Mechanism for proton conduction of the M(2) ion channel of influenza A virus

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

Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly.

The M2 ectodomain is important for its incorporation into influenza A virions.

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12283-12288

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10.1073/PNAS.0905726106

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106

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William DeGrado

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2009-07-09T00:00:00Z

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