A computational study of the closed and open states of the influenza a M2 proton channel.
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Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A VirusModeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Free-energy profiles for ions in the influenza M2-TMD channelProton transport behavior through the influenza A M2 channel: insights from molecular simulation.Proton transport through influenza A virus M2 protein reconstituted in vesicles.Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulationsThe interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus.Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza A virus.Ab initio calculations and validation of the pH-dependent structures of the His37-Trp41 quartet, the heart of acid activation and proton conductance in the M2 protein of Influenza A virusExploring Histidine Conformations in the M2 Channel Lumen of the Influenza A Virus at Neutral pH via Molecular SimulationsA secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine.Activation and proton transport mechanism in influenza A M2 channelAcid activation mechanism of the influenza A M2 proton channel.Structure and function of the influenza A M2 proton channelStructural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Equilibrium exchange processes of the aqueous tryptophan dipeptide.Application of solid-state NMR restraint potentials in membrane protein modeling.Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel.Computational studies of gramicidin permeation: an entry way sulfonate enhances cation occupancy at entry sites.Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers.Water is an active matrix of life for cell and molecular biology.
P2860
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P2860
A computational study of the closed and open states of the influenza a M2 proton channel.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
A computational study of the closed and open states of the influenza a M2 proton channel.
@ast
A computational study of the closed and open states of the influenza a M2 proton channel.
@en
type
label
A computational study of the closed and open states of the influenza a M2 proton channel.
@ast
A computational study of the closed and open states of the influenza a M2 proton channel.
@en
prefLabel
A computational study of the closed and open states of the influenza a M2 proton channel.
@ast
A computational study of the closed and open states of the influenza a M2 proton channel.
@en
P2860
P1433
P1476
A computational study of the closed and open states of the influenza a M2 proton channel.
@en
P2093
P2860
P304
P356
10.1529/BIOPHYSJ.105.066647
P407
P577
2005-07-22T00:00:00Z