KCNQ1 channels voltage dependence through a voltage-dependent binding of the S4-S5 linker to the pore domain.
about
Cellular mechanisms of mutations in Kv7.1: auditory functions in Jervell and Lange-Nielsen syndrome vs. Romano-Ward syndromeWorking model for the structural basis for KCNE1 modulation of the KCNQ1 potassium channel.Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome.PIP₂-dependent coupling is prominent in Kv7.1 due to weakened interactions between S4-S5 and S6.Demonstration of physical proximity between the N terminus and the S4-S5 linker of the human ether-a-go-go-related gene (hERG) potassium channelDouble mutant cycle analysis identified a critical leucine residue in the IIS4S5 linker for the activation of the Ca(V)2.3 calcium channel.A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel.Opposite Effects of the S4-S5 Linker and PIP(2) on Voltage-Gated Channel Function: KCNQ1/KCNE1 and Other Channels.Coupling of voltage-sensors to the channel pore: a comparative viewMutations in cytoplasmic loops of the KCNQ1 channel and the risk of life-threatening events: implications for mutation-specific response to β-blocker therapy in type 1 long-QT syndrome.Aromatic-aromatic interactions between residues in KCa3.1 pore helix and S5 transmembrane segment control the channel gating process.Gating mechanisms underlying deactivation slowing by two KCNQ1 atrial fibrillation mutations.Cytoplasmic domains and voltage-dependent potassium channel gating.Mechanism of electromechanical coupling in voltage-gated potassium channels.Being flexible: the voltage-controllable activation gate of kv channels.Potassium channels: structures, diseases, and modulators.Genetics of sudden cardiac death caused by ventricular arrhythmias.Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channelVoltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Molecular Pathophysiology of Congenital Long QT Syndrome.An allosteric mechanism for drug block of the human cardiac potassium channel KCNQ1.The S4-S5 linker of KCNQ1 channels forms a structural scaffold with the S6 segment controlling gate closureStructural modelling and mutant cycle analysis predict pharmacoresponsiveness of a Na(V)1.7 mutant channel.hERG S4-S5 linker acts as a voltage-dependent ligand that binds to the activation gate and locks it in a closed stateStudying Kv Channels Function using Computational Methods.
P2860
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P2860
KCNQ1 channels voltage dependence through a voltage-dependent binding of the S4-S5 linker to the pore domain.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@ast
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@en
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@nl
type
label
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@ast
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@en
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@nl
prefLabel
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@ast
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@en
KCNQ1 channels voltage depende ...... -S5 linker to the pore domain.
@nl
P2093
P2860
P50
P356
P1476
KCNQ1 channels voltage depende ...... 4-S5 linker to the pore domain
@en
P2093
Alain J Labro
Carole Le Hénaff
Denis Escande
Fayal Abderemane Ali
Frank S Choveau
Hélène Boudin
Jean Mérot
Shehrazade Dahimène
P2860
P304
P356
10.1074/JBC.M110.146324
P407
P577
2010-10-12T00:00:00Z