Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.
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Insight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channelA recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channelsStructural Basis for the cAMP-dependent Gating in the Human HCN4 ChannelMechanistic Insight into Human ether-a-go-go-related Gene (hERG) K+ Channel Deactivation Gating from the Solution Structure of the EAG DomainThe S4–S5 Linker Acts as a Signal Integrator for hERG K+ Channel Activation and Deactivation GatingA structural basis for drug-induced long QT syndromeRegulation of an ERG K+ current by Src tyrosine kinaseMolecular determinants of interactions between the N-terminal domain and the transmembrane core that modulate hERG K+ channel gating.A single histidine residue determines the pH sensitivity of the pacemaker channel HCN2.Novel characteristics of a misprocessed mutant HERG channel linked to hereditary long QT syndrome.Inherited and acquired vulnerability to ventricular arrhythmias: cardiac Na+ and K+ channels.Use of mutant-specific ion channel characteristics for risk stratification of long QT syndrome patients.Proline scan of the HERG channel S6 helix reveals the location of the intracellular pore gate.The S4-S5 linker couples voltage sensing and activation of pacemaker channels.Modulation of the ERG K+ current by the tyrosine phosphatase, SHP-1.Effect of S6 tail mutations on charge movement in Shaker potassium channelsMutations within the S4-S5 linker alter voltage sensor constraints in hERG K+ channels.The Eag domain regulates the voltage-dependent inactivation of rat Eag1 K+ channels.The cooperative voltage sensor motion that gates a potassium channel.Demonstration of physical proximity between the N terminus and the S4-S5 linker of the human ether-a-go-go-related gene (hERG) potassium channelStructural basis of action for a human ether-a-go-go-related gene 1 potassium channel activator.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 viewVoltage-sensing domain mode shift is coupled to the activation gate by the N-terminal tail of hERG channelsDetection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conductionTrapping of a methanesulfonanilide by closure of the HERG potassium channel activation gate.Molecular coupling between voltage sensor and pore opening in the Arabidopsis inward rectifier K+ channel KAT1.Perspectives on: conformational coupling in ion channels: thermodynamics of electromechanical coupling in voltage-gated ion channels.Homology model and targeted mutagenesis identify critical residues for arachidonic acid inhibition of Kv4 channelsHydrophobic interactions between the voltage sensor and pore mediate inactivation in Kv11.1 channels.Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels.Transfer of rolf S3-S4 linker to HERG eliminates activation gating but spares inactivation.Stereoselective Blockage of Quinidine and Quinine in the hERG Channel and the Effect of Their Rescue Potency on Drug-Induced hERG Trafficking Defect.HERG potassium channel regulation by the N-terminal eag domain.Voltage-dependent gating of HERG potassium channels.Mechanism of electromechanical coupling in voltage-gated potassium channels.A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency.Activation of Slo2.1 channels by niflumic acid.Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains.Molecular determinants of voltage-dependent human ether-a-go-go related gene (HERG) K+ channel block.
P2860
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P2860
Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@en
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@nl
type
label
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@en
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@nl
prefLabel
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@en
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@nl
P2860
P1476
Mutations of the S4-S5 linker ...... expressed in Xenopus oocytes.
@en
P2093
M C Sanguinetti
P2860
P304
P356
10.1111/J.1469-7793.1999.667AD.X
P407
P478
514 ( Pt 3)
P577
1999-02-01T00:00:00Z