Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity. - Wikidata - awgldk - TriplyDB

Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

http://www.wikidata.org/entity/Q34598265

about

Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel 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 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 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 Influenza M2 proton channels Designing inhibitors of M2 proton channel against H1N1 swine influenza virus Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis Philosophy of voltage-gated proton channels Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel Solid state NMR: The essential technology for helical membrane protein structural characterization.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.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.Considering protonation as a posttranslational modification regulating protein structure and function.Solid state NMR strategy for characterizing native membrane protein structures Emerging antiviral strategies to interfere with influenza virus entry.Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts 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.Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Probing Hydronium Ion Histidine NH Exchange Rate Constants in the M2 Channel via Indirect Observation of Dipolar-Dephased 15N Signals in Magic-Angle-Spinning NMR.Free-energy profiles for ions in the influenza M2-TMD channel 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 Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.A histidine-rich linker region in peptidylglycine α-amidating monooxygenase has the properties of a pH sensor.Impact of histidine residues on the transmembrane helices of viroporins.Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR

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Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

http://www.wikidata.org/entity/Q34598265

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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Histidines, heart of the hydro ...... ctance and proton selectivity.

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

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Histidines, heart of the hydro ...... uctance and proton selectivity

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David D Busath

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Huan-Xiang Zhou

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Jun Hu

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Li Zhang

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Riqiang Fu

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Timothy A Cross

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Viksita Vijayvergiya

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P2860

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

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

Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus

A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment

A low-barrier hydrogen bond in the catalytic triad of serine proteases

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.

Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.

Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus

Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation

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6865-6870

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10.1073/PNAS.0601944103

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18

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103

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Katsuyuki Nishimura

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2006-04-21T00:00:00Z

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7147407

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16632600

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