Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.
about
Magic angle spinning NMR of virusesSolid-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.Flipping in the pore: discovery of dual inhibitors that bind in different orientations to the wild-type versus the amantadine-resistant S31N mutant of the influenza A virus M2 proton channel.Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).NMR studies of active-site properties of human carbonic anhydrase II by using (15) N-labeled 4-methylimidazole as a local probe and histidine hydrogen-bond correlations.The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conductionMultiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Preparation of a novel rape pollen shell microencapsulation and its use for protein adsorption and pH-controlled release.Effect of cytosolic pH on inward currents reveals structural characteristics of the proton transport cycle in the influenza A protein M2 in cell-free membrane patches of Xenopus oocytesDiscovery of Highly Potent Inhibitors Targeting the Predominant Drug-Resistant S31N Mutant of the Influenza A Virus M2 Proton Channel.Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers.Acid activation mechanism of the influenza A M2 proton channel.Mechanisms of Action of Novel Influenza A/M2 Viroporin Inhibitors Derived from Hexamethylene Amiloride.Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.Slow but Steady Wins the Race: Dissimilarities among New Dual Inhibitors of the Wild-Type and the V27A Mutant M2 Channels of Influenza A Virus.Pharmacological Characterization of the Spectrum of Antiviral Activity and Genetic Barrier to Drug Resistance of M2-S31N Channel Blockers.3-Azatetracyclo[5.2.1.1(5,8).0(1,5)]undecane derivatives: from wild-type inhibitors of the M2 ion channel of influenza A virus to derivatives with potent activity against the V27A mutant.Generation of an 4-Isoxazolyl Anion Species: Facile Access to Multifunctionalized Isoxazoles.Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.
P2860
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P2860
Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Drug-induced conformational an ...... vestigated by solid-state NMR.
@ast
Drug-induced conformational an ...... vestigated by solid-state NMR.
@en
type
label
Drug-induced conformational an ...... vestigated by solid-state NMR.
@ast
Drug-induced conformational an ...... vestigated by solid-state NMR.
@en
prefLabel
Drug-induced conformational an ...... vestigated by solid-state NMR.
@ast
Drug-induced conformational an ...... vestigated by solid-state NMR.
@en
P2093
P2860
P356
P1476
Drug-induced conformational an ...... vestigated by solid-state NMR.
@en
P2093
Daniel Tietze
Jonathan K Williams
P2860
P304
P356
10.1021/JA4041412
P407
P577
2013-06-21T00:00:00Z