Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels. - Wikidata - wikimedia - TriplyDB

Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels.

Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels.

http://www.wikidata.org/entity/Q37055488

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The hitchhiker's guide to the voltage-gated sodium channel galaxy Na+ channel function, regulation, structure, trafficking and sequestration Resurgent current of voltage-gated Na(+) channels A distinct sodium channel voltage-sensor locus determines insect selectivity of the spider toxin Dc1a Independent movement of the voltage sensors in KV2.1/KV6.4 heterotetramers Structure and function of voltage-gated sodium channels at atomic resolution.Synergetic action of domain II and IV underlies persistent current generation in Nav1.3 as revealed by a tarantula toxin.Cardiac Na Channels: Structure to Function The tarantula toxin β/δ-TRTX-Pre1a highlights the importance of the S1-S2 voltage-sensor region for sodium channel subtype selectivity.Insect-Active Toxins with Promiscuous Pharmacology from the African Theraphosid Spider Monocentropus balfouri Gating-pore currents demonstrate selective and specific modulation of individual sodium channel voltage-sensors by biological toxins.Pyrethroids differentially alter voltage-gated sodium channels from the honeybee central olfactory neurons.Functional heterogeneity of the four voltage sensors of a human L-type calcium channel A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif.Electrophysiological characteristics of a SCN5A voltage sensors mutation R1629Q associated with Brugada syndrome Defective fast inactivation recovery of Nav 1.4 in congenital myasthenic syndrome.Binary architecture of the Nav1.2-β2 signaling complex Temperature-dependent changes in neuronal dynamics in a patient with an SCN1A mutation and hyperthermia induced seizures A first exploration of the venom of the Buthus occitanus scorpion found in southern France.Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.A new look at sodium channel β subunits Conservation of alternative splicing in sodium channels reveals evolutionary focus on release from inactivation and structural insights into gating.Pharmacology of the Nav1.1 domain IV voltage sensor reveals coupling between inactivation gating processes.Molecular Pathophysiology of Congenital Long QT Syndrome.Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.Depolarization of the conductance-voltage relationship in the NaV1.5 mutant, E1784K, is due to altered fast inactivation.Domain III S4 in closed-state fast inactivation: insights from a periodic paralysis mutation Mechanisms of noncovalent β subunit regulation of NaV channel gating.What activates inactivation?Structures of closed and open states of a voltage-gated sodium channel.Regulation of Na+ channel inactivation by the DIII and DIV voltage-sensing domains.Upward movement of IS4 and IIIS4 is a rate-limiting stage in Cav1.2 activation.Key role of segment IS4 in Cav1.2 inactivation: link between activation and inactivation.Direct Measurement of Cardiac Na+ Channel Conformations Reveals Molecular Pathologies of Inherited Mutations.Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation.Mechanisms of Drug Binding to Voltage-Gated Sodium Channels.The Selective Nav1.7 Inhibitor, PF-05089771, Interacts Equivalently with Fast and Slow Inactivated Nav1.7 Channels.Design of sodium channel ligands with defined selectivity - a case study in scorpion alpha-toxins.A perspective on Na and K channel inactivation.Structural and Functional Analysis of Sodium Channels Viewed from an Evolutionary Perspective.

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P2860

Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels.

http://www.wikidata.org/entity/Q37055488

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 July 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Domain IV voltage-sensor movem ...... activation in sodium channels.

@en

Domain IV voltage-sensor movem ...... activation in sodium channels.

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type

label

Domain IV voltage-sensor movem ...... activation in sodium channels.

@en

Domain IV voltage-sensor movem ...... activation in sodium channels.

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Domain IV voltage-sensor movem ...... activation in sodium channels.

@en

Domain IV voltage-sensor movem ...... activation in sodium channels.

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The Journal of General Physiology

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Domain IV voltage-sensor movem ...... nactivation in sodium channels

@en

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Deborah L Capes

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

Francisco Bezanilla

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

Marcel P Goldschen-Ohm

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

P2860

A quantitative description of membrane current and its application to conduction and excitation in nerve

SCN5A mutations associated with an inherited cardiac arrhythmia, long QT syndrome

Radicals r'aging.

Cardiac sodium channel mutations in patients with long QT syndrome, an inherited cardiac arrhythmia.

The long QT syndrome: ion channel diseases of the heart.

The Na channel voltage sensor associated with inactivation is localized to the external charged residues of domain IV, S4.

The voltage sensor in voltage-dependent ion channels.

Molecular determinants of coupling between the domain III voltage sensor and pore of a sodium channel

Interaction between the sodium channel inactivation linker and domain III S4-S5.

A sodium channel gating model based on single channel, macroscopic ionic, and gating currents in the squid giant axon

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101-112

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scholarly article

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10.1085/JGP.201310998

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2

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142

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Manoel Arcisio-Miranda

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2013-07-15T00:00:00Z

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249648957

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23858005

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3727307

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