Cu(II) inhibition of the proton translocation machinery of the influenza A virus M2 protein.
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Determinants of Hepatitis C Virus p7 Ion Channel Function and Drug Sensitivity Identified In VitroDetermination of Pore-Lining Residues in the Hepatitis C Virus p7 ProteinBackbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A VirusStructural basis for the function and inhibition of an influenza virus proton channelMechanism for proton conduction of the M(2) ion channel of influenza A virusThe gate of the influenza virus M2 proton channel is formed by a single tryptophan residueChemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virusDesign novel dual agonists for treating type-2 diabetes by targeting peroxisome proliferator-activated receptors with core hopping approachpH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virusParamagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Structural basis for proton conduction and inhibition by the influenza M2 protein.Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.A computational study of the closed and open states of the influenza a M2 proton channel.Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMRAnalysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility methodEffect of cytoplasmic tail truncations on the activity of the M(2) ion channel of influenza A virus.2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel.Computational study of drug binding to the membrane-bound tetrameric M2 peptide bundle from influenza A virusControlling influenza virus replication by inhibiting its proton channel.Specific cell ablation in Drosophila using the toxic viral protein M2(H37A).Computational studies of proton transport through the M2 channel.Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus.The chemical and dynamical influence of the anti-viral drug amantadine on the M2 proton channel transmembrane domain.The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels.Solid-supported membrane technology for the investigation of the influenza A virus M2 channel activityThe interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus.Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine.Structure and function of the influenza A M2 proton channelHost Cell Copper Transporters CTR1 and ATP7A are important for Influenza A virus replication.Flu channel drug resistance: a tale of two sites.Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.Find novel dual-agonist drugs for treating type 2 diabetes by means of cheminformatics.Design and pharmacological characterization of inhibitors of amantadine-resistant mutants of the M2 ion channel of influenza A virusActivation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Investigation of the free energy profiles of amantadine and rimantadine in the AM2 binding pocket.Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5).
P2860
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P2860
Cu(II) inhibition of the proton translocation machinery of the influenza A virus M2 protein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Cu(II) inhibition of the proto ...... influenza A virus M2 protein.
@en
type
label
Cu(II) inhibition of the proto ...... influenza A virus M2 protein.
@en
prefLabel
Cu(II) inhibition of the proto ...... influenza A virus M2 protein.
@en
P2093
P2860
P356
P1476
Cu(II) inhibition of the proto ...... influenza A virus M2 protein.
@en
P2093
DeGrado WF
Dieckmann GR
P2860
P304
P356
10.1074/JBC.274.9.5474
P407
P577
1999-02-01T00:00:00Z