The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer.
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Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channelAccurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivativesStructure of the transmembrane region of the M2 protein H+ channelStructure 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 BindingMechanism 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 viruspH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virusNovel strategies for prevention and treatment of influenza.Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Cooperativity and specificity of association of a designed transmembrane peptide.Uniformity, ideality, and hydrogen bonds in transmembrane alpha-helices.Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).A computational study of the closed and open states of the influenza a M2 proton channel.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.Viral ion channels: molecular modeling and simulation.Endoplasmic reticulum-localized human papillomavirus type 16 E5 protein alters endosomal pH but not trans-Golgi pH.Effect of cleavage mutants on syncytium formation directed by the wild-type fusion protein of Newcastle disease virusAnalysis 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.Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientationCoexistence of two adamantane binding sites in the influenza A M2 ion channel.Influenza a virus M2 ion channel activity is essential for efficient replication in tissue culture.Evidence for dimerization of dimers in K+ channel assembly.Computer simulation of ion channel gating: the M(2) channel of influenza A virus in a lipid bilayer.AFM visualization of mobile influenza A M2 molecules in planar bilayersProton conductance of influenza virus M2 protein in planar lipid bilayers.The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivativesUse of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.Multiple Proton Confinement in the M2 Channel from the Influenza A VirusM2e-displaying virus-like particles with associated RNA promote T helper 1 type adaptive immunity against influenza A.Effect of cysteine mutations in the extracellular domain of CM2 on the influenza C virus replication.How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles.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.
P2860
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P2860
The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The active oligomeric state of ...... M2 ion channel is a tetramer.
@ast
The active oligomeric state of ...... M2 ion channel is a tetramer.
@en
type
label
The active oligomeric state of ...... M2 ion channel is a tetramer.
@ast
The active oligomeric state of ...... M2 ion channel is a tetramer.
@en
prefLabel
The active oligomeric state of ...... M2 ion channel is a tetramer.
@ast
The active oligomeric state of ...... M2 ion channel is a tetramer.
@en
P2860
P356
P1476
The active oligomeric state of ...... s M2 ion channel is a tetramer
@en
P2860
P304
P356
10.1073/PNAS.94.10.5000
P407
P577
1997-05-01T00:00:00Z