Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.
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Obstructing toxin pathways by targeted pore blockageViral Membrane Channels: Role and Function in the Virus Life CycleStructural basis for the function and inhibition of an influenza virus proton channelStructure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virusStructure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virusHigh-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transductionAn assay suitable for high throughput screening of anti-influenza drugsFlipping 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.Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.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.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.The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conductionPore hydration states of KcsA potassium channels in membranesInfluenza 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.2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel.Diffusion-Influenced Transport of Ions across a Transmembrane Channel with an Internal Binding Site.Aminoadamantanes with persistent in vitro efficacy against H1N1 (2009) influenza ANMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.Coexistence of two adamantane binding sites in the influenza A M2 ion channel.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 virusMultiple Proton Confinement in the M2 Channel from the Influenza A VirusTidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Viral miniproteinsInfluence of solubilizing environments on membrane protein structuresA pH-dependent conformational ensemble mediates proton transport through the influenza A/M2 proteinEffect of cytosolic pH on inward currents reveals structural characteristics of the proton transport cycle in the influenza A protein M2 in cell-free membrane patches of Xenopus oocytesHydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.Proton affinity of the histidine-tryptophan cluster motif from the influenza A virus from ab initio molecular dynamics.Full Genome Characterization of Human Influenza A/H3N2 Isolates from Asian Countries Reveals a Rare Amantadine Resistance-Conferring Mutation and Novel PB1-F2 Polymorphisms.Discovery of Highly Potent Inhibitors Targeting the Predominant Drug-Resistant S31N Mutant of the Influenza A Virus M2 Proton Channel.Influenza matrix protein 2 alters CFTR expression and function through its ion channel activity.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 SimulationsAsp44 stabilizes the Trp41 gate of the M2 proton channel of influenza A virus.Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.
P2860
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P2860
Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Functional studies and modelin ...... luenza a virus M2 ion channel.
@en
Functional studies and modelin ...... luenza a virus M2 ion channel.
@nl
type
label
Functional studies and modelin ...... luenza a virus M2 ion channel.
@en
Functional studies and modelin ...... luenza a virus M2 ion channel.
@nl
prefLabel
Functional studies and modelin ...... luenza a virus M2 ion channel.
@en
Functional studies and modelin ...... luenza a virus M2 ion channel.
@nl
P2093
P2860
P356
P1433
P1476
Functional studies and modelin ...... luenza a virus M2 ion channel.
@en
P2093
Giacomo Fiorin
Lawrence H Pinto
Michael L Klein
Robert A Lamb
Victoria Balannik
Vincenzo Carnevale
William F Degrado
P2860
P304
P356
10.1021/BI901799K
P407
P577
2010-02-01T00:00:00Z