Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein.
about
Magic angle spinning NMR of virusesM2 protein from influenza A: from multiple structures to biophysical and functional insightsFunctional characterization of a melittin analog containing a non-natural tryptophan analogStructural basis for the function and inhibition of an influenza virus proton channelSolid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton ChannelProbing membrane protein structure using water polarization transfer solid-state NMR.Membrane protein structure and dynamics from NMR spectroscopy.Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.Structural basis for proton conduction and inhibition by the influenza M2 protein.Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRpH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMRDrug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conductionChemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domainLipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivativesHydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.Topical Developments in High-Field Dynamic Nuclear Polarization.NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide.Investigation of the curvature induction and membrane localization of the influenza virus M2 protein using static and off-magic-angle spinning solid-state nuclear magnetic resonance of oriented bicelles.Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes.Dynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional MechanismCholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.Efficient DNP NMR of membrane proteins: sample preparation protocols, sensitivity, and radical location.Helical membrane protein conformations and their environmentThe Application of REDOR NMR to Understand the Conformation of Epothilone B.Affinity of Rimantadine Enantiomers against Influenza A/M2 Protein Revisited.Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Dynamic nuclear polarization study of inhibitor binding to the M2(18-60) proton transporter from influenza A.Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling.Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.Strategies for Efficient Sample Preparation for Dynamic Nuclear Polarization Solid-State NMR of Biological Macromolecules.A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity to Cholesterol, and Perturbed Interdomain Coupling.Conformation and topology of diacylglycerol kinase in E.coli membranes revealed by solid-state NMR spectroscopy.
P2860
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P2860
Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Membrane-dependent effects of ...... he influenza virus M2 protein.
@en
Membrane-dependent effects of ...... he influenza virus M2 protein.
@nl
type
label
Membrane-dependent effects of ...... he influenza virus M2 protein.
@en
Membrane-dependent effects of ...... he influenza virus M2 protein.
@nl
prefLabel
Membrane-dependent effects of ...... he influenza virus M2 protein.
@en
Membrane-dependent effects of ...... he influenza virus M2 protein.
@nl
P2860
P356
P1476
Membrane-dependent effects of ...... the influenza virus M2 protein
@en
P2093
P2860
P304
11572-11579
P356
10.1021/JA202051N
P407
P577
2011-07-07T00:00:00Z