The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR
about
Quantification of helix-helix binding affinities in micelles and lipid bilayersStructure determination of membrane proteins by nuclear magnetic resonance spectroscopyMagic angle spinning NMR of virusesM2 protein from influenza A: from multiple structures to biophysical and functional insightsComputable features required to evaluate the efficacy of drugs and a universal algorithm to find optimally effective drug in a drug complexBackbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A VirusConformational changes induced by a single amino acid substitution in thetrans-membrane domain of Vpu: Implications for HIV-1 susceptibility to channel blocking drugsBackbone structure of a small helical integral membrane protein: A unique structural characterizationInsight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid BilayerStructure Determination of a Membrane Protein in ProteoliposomesBinding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural StudySolid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton ChannelMembrane protein structure determination: back to the membrane.Solid state NMR: The essential technology for helical membrane protein structural characterization.Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Assembly of the m2 tetramer is strongly modulated by lipid chain length.Optimal mutation sites for PRE data collection and membrane protein structure prediction.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.Solid state NMR strategy for characterizing native membrane protein structurespH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMRSolid state NMR and protein-protein interactions in membranesProton 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.Free-energy profiles for ions in the influenza M2-TMD channelDiscovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.Conformational heterogeneity of the M2 proton channel and a structural model for channel activationMechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMRA theory for the proton transport of the influenza virus M2 protein: extensive test against conductance dataMultiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Where does amantadine bind to the influenza virus M2 proton channel?Proton conductance of influenza virus M2 protein in planar lipid bilayers.Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domainHistidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.Controlling influenza virus replication by inhibiting its proton channel.Multiple Proton Confinement in the M2 Channel from the Influenza A Virus
P2860
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P2860
The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The closed state of a H+ chann ...... estraints from solid state NMR
@ast
The closed state of a H+ chann ...... estraints from solid state NMR
@en
The closed state of a H+ chann ...... estraints from solid state NMR
@nl
type
label
The closed state of a H+ chann ...... estraints from solid state NMR
@ast
The closed state of a H+ chann ...... estraints from solid state NMR
@en
The closed state of a H+ chann ...... estraints from solid state NMR
@nl
prefLabel
The closed state of a H+ chann ...... estraints from solid state NMR
@ast
The closed state of a H+ chann ...... estraints from solid state NMR
@en
The closed state of a H+ chann ...... estraints from solid state NMR
@nl
P356
P1433
P1476
The closed state of a H+ chann ...... estraints from solid state NMR
@en
P2093
P304
13170-13177
P356
10.1021/BI0262799
P407
P577
2002-11-01T00:00:00Z