The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction
about
The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic ResonanceSolid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton ChannelHeating and temperature gradients of lipid bilayer samples induced by RF irradiation in MAS solid-state NMR experiments.Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH JumpDynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional MechanismBeyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.Acid activation mechanism of the influenza A M2 proton channel.XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Activation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.Functional studies reveal the similarities and differences between AM2 and BM2 proton channels from influenza viruses.Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.Voltage and pH sensing by the voltage-gated proton channel, HV1.
P2860
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P2860
The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction
description
2015 nî lūn-bûn
@nan
2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@ast
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@en
type
label
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@ast
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@en
prefLabel
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@ast
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@en
P2860
P50
P356
P1476
The influenza m2 cytoplasmic t ...... o facilitate proton conduction
@en
P2093
Shu Y Liao
P2860
P304
P356
10.1021/JACS.5B02510
P407
P577
2015-04-30T00:00:00Z