Fast inactivation causes rectification of the IKr channel. - Wikidata - awgldk - TriplyDB

Fast inactivation causes rectification of the IKr channel.

Fast inactivation causes rectification of the IKr channel.

http://www.wikidata.org/entity/Q36411776

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Cloning and functional expression of two families of beta-subunits of the large conductance calcium-activated K+ channel Voltage-dependent inactivation of the human K+ channel KvLQT1 is eliminated by association with minimal K+ channel (minK) subunits A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels Mechanistic Insight into Human ether-a-go-go-related Gene (hERG) K+ Channel Deactivation Gating from the Solution Structure of the EAG Domain Mechanism of Cd2+ Coordination during Slow Inactivation in Potassium Channels The S4–S5 Linker Acts as a Signal Integrator for hERG K+ Channel Activation and Deactivation Gating Calmodulin Regulates Human Ether à Go-Go 1 (hEAG1) Potassium Channels through Interactions of the Eag Domain with the Cyclic Nucleotide Binding Homology Domain Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel State-dependent barium block of wild-type and inactivation-deficient HERG channels in Xenopus oocytes Rate dependency of delayed rectifier currents during the guinea-pig ventricular action potential Modulation of rat erg1, erg2, erg3 and HERG K+ currents by thyrotropin-releasing hormone in anterior pituitary cells via the native signal cascade Regulation of the human ether-a-gogo related gene (HERG) K+ channels by reactive oxygen species Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-à-go-go potassium channel Properties of HERG channels stably expressed in HEK 293 cells studied at physiological temperature Changes in channel trafficking and protein stability caused by LQT2 mutations in the PAS domain of the HERG channel Cloning of a mammalian elk potassium channel gene and EAG mRNA distribution in rat sympathetic ganglia Regulation of an ERG K+ current by Src tyrosine kinase Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods Molecular driving forces determining potassium channel slow inactivation.Molecular determinants of interactions between the N-terminal domain and the transmembrane core that modulate hERG K+ channel gating.A new C-terminal hERG mutation A915fs+47X associated with symptomatic LQT2 and auditory-trigger syncope Overlapping LQT1 and LQT2 phenotype in a patient with long QT syndrome associated with loss-of-function variations in KCNQ1 and KCNH2 The S1 helix critically regulates the finely tuned gating of Kv11.1 channels Dysfunction of delayed rectifier potassium channels in an inherited cardiac arrhythmia.The eag family of K+ channels in Drosophila and mammals.K+ channel inactivation mediated by the concerted action of the cytoplasmic N- and C-terminal domains.HERG1 channelopathies Pacemaker oscillations in heart and brain: a key role for hyperpolarization-activated cation channels.Concerted all-or-none subunit interactions mediate slow deactivation of human ether-à-go-go-related gene K+ channels Modulation of the ERG K+ current by the tyrosine phosphatase, SHP-1.Effects of divalent cations on the E-4031-sensitive repolarization current, I(Kr), in rabbit ventricular myocytes.The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field.Evidence for multiple open and inactivated states of the hKv1.5 delayed rectifier Activation and inactivation of homomeric KvLQT1 potassium channels.Blockade of HERG channels expressed in Xenopus laevis oocytes by external divalent cations.Effects of outer mouth mutations on hERG channel function: a comparison with similar mutations in the Shaker channel.Proton and zinc effects on HERG currents Enhancement of HERG K+ currents by Cd2+ destabilization of the inactivated state.BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1 Mutations within the S4-S5 linker alter voltage sensor constraints in hERG K+ channels.

P2860

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P2860

Fast inactivation causes rectification of the IKr channel.

http://www.wikidata.org/entity/Q36411776

description

1996 nî lūn-bûn

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1996年の論文

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

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1996年學術文章

@zh-hant

name

Fast inactivation causes rectification of the IKr channel.

@ast

Fast inactivation causes rectification of the IKr channel.

@en

type

label

Fast inactivation causes rectification of the IKr channel.

@ast

Fast inactivation causes rectification of the IKr channel.

@en

prefLabel

Fast inactivation causes rectification of the IKr channel.

@ast

Fast inactivation causes rectification of the IKr channel.

@en

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The Journal of General Physiology

P1476

Fast inactivation causes rectification of the IKr channel.

@en

P2093

A Zou

http://www.w3.org/2001/XMLSchema#string

M C Sanguinetti

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M E Curran

http://www.w3.org/2001/XMLSchema#string

M T Keating

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P S Spector

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P2860

A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel

A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome

HERG, a human inward rectifier in the voltage-gated potassium channel family

Biophysical and molecular mechanisms of Shaker potassium channel inactivation

Repolarization currents in embryonic chick atrial heart cell aggregates

Inward rectification of a potassium channel in cardiac ventricular cells depends on internal magnesium ions

Regulation of voltage dependence of the KAT1 channel by intracellular factors.

Two components of cardiac delayed rectifier K+ current. Differential sensitivity to block by class III antiarrhythmic agents.

Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae.

Magnesium-independent activation of inward-rectifying K+ channels in Vicia faba guard cells.

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611-619

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10.1085/JGP.107.5.611

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5

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107

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1996-05-01T00:00:00Z

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8740374

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2217012

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