Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus - Test2 - elhamkhani - TriplyDB

Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus

Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus

http://www.wikidata.org/entity/Q27663887

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Aspartate 112 is the selectivity filter of the human voltage-gated proton channel Relevance of Viroporin Ion Channel Activity on Viral Replication and Pathogenesis M2 protein from influenza A: from multiple structures to biophysical and functional insights NMR structures of membrane proteins in phospholipid bilayers Principles of virus structural organization Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductase Structural basis for the function and inhibition of an influenza virus proton channel Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction Inhibitors of the influenza A virus M2 proton channel discovered using a high-throughput yeast growth restoration assay Philosophy of voltage-gated proton channels Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic Resonance Progress of small molecular inhibitors in the development of anti-influenza virus agents.Probing membrane protein structure using water polarization transfer solid-state NMR.Flipping in the pore: discovery of dual inhibitors that bind in different orientations to the wild-type versus the amantadine-resistant S31N mutant of the influenza A virus M2 proton channel.Influenza virus M2 protein ion channel activity helps to maintain pandemic 2009 H1N1 virus hemagglutinin fusion competence during transport to the cell surface.Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared 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.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.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.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.pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMR 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.Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).Pore hydration states of KcsA potassium channels in membranes A theory for the proton transport of the influenza virus M2 protein: extensive test against conductance data Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel.NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain Voltage-gated proton channels.Multiple Proton Confinement in the M2 Channel from the Influenza A Virus Human monoclonal ScFv that bind to different functional domains of M2 and inhibit H5N1 influenza virus replication.CFTR and lung homeostasis.

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Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus

http://www.wikidata.org/entity/Q27663887

description

2010 nî lūn-bûn

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2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2010 թվականի օգոստոսին հրատարակված գիտական հոդված

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2010年の論文

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2010年论文

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

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Structure and mechanism of pro ...... undle of the influenza A virus

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Alexei L Polishchuk

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Giacomo Fiorin

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Lawrence H Pinto

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Michael L Klein

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Robert A Lamb

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Rudresh Acharya

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Victoria Balannik

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Vincenzo Carnevale

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P2860

Existing antivirals are effective against influenza viruses with genes from the 1918 pandemic virus.

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

Comparison of simple potential functions for simulating liquid water

Control of the selectivity of the aquaporin water channel family by global orientational tuning

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

Mechanism of drug inhibition and drug resistance of influenza A M2 channel

Structure of a tetrameric MscL in an expanded intermediate state

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107

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Benjamin G Levine

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45508442

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transmembrane transport

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protein structure

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