Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
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The voltage-dependent gate in MthK potassium channels is located at the selectivity filterStructures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding SiteSelection of inhibitor-resistant viral potassium channels identifies a selectivity filter site that affects barium and amantadine blockStructural correlates of selectivity and inactivation in potassium channels.Computational study of drug binding to the membrane-bound tetrameric M2 peptide bundle from influenza A virusFluorescent system based on bacterial expression of hybrid KcsA channels designed for Kv1.3 ligand screening and study.The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations and Shaker B inactivation peptides.A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism.Stabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanismTrans-channel interactions in batrachotoxin-modified skeletal muscle sodium channels: voltage-dependent block by cytoplasmic amines, and the influence of mu-conotoxin GIIIA derivatives and permeant ionsMolecular template for a voltage sensor in a novel K+ channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channelInteraction of local anesthetics with the K (+) channel pore domain: KcsA as a model for drug-dependent tetramer stabilityTransmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.K+ channel modulators for the treatment of neurological disorders and autoimmune diseasesFlu channel drug resistance: a tale of two sites.Surface-enhanced IR absorption spectroscopy of the KcsA potassium channel upon application of an electric field.K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.K(+) channels of squid giant axons open by an osmotic stress in hypertonic solutions containing nonelectrolytes.
P2860
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P2860
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
description
2007 nî lūn-bûn
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2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2007 թվականի փետրվարին հրատարակված գիտական հոդված
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年學術文章
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name
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@ast
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@en
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@nl
type
label
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@ast
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@en
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@nl
prefLabel
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@ast
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@en
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@nl
P2093
P1476
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
@en
P2093
Sarah Yohannan
Yufeng Zhou
P304
P356
10.1016/J.JMB.2006.11.081
P407
P577
2007-02-23T00:00:00Z