How does the W434F mutation block current in Shaker potassium channels? - Wikidata - awgldk - TriplyDB

How does the W434F mutation block current in Shaker potassium channels?

How does the W434F mutation block current in Shaker potassium channels?

http://www.wikidata.org/entity/Q36411800

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Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition Mechanism of Cd2+ Coordination during Slow Inactivation in Potassium Channels U-type inactivation of Kv3.1 and Shaker potassium channels.A single residue differentiates between human cardiac and skeletal muscle Na+ channel slow inactivation Modification of voltage-dependent gating of potassium channels by free form of tryptophan side chain.Gating currents from a Kv3 subfamily potassium channel: charge movement and modification by BDS-II toxin K⁺ channel gating: C-type inactivation is enhanced by calcium or lanthanum outside Structural correlates of selectivity and inactivation in potassium channels.Shedding light on voltage-dependent gating.Use of voltage clamp fluorimetry in understanding potassium channel gating: a review of Shaker fluorescence data.Moving gating charges through the gating pore in a Kv channel voltage sensor.Concerted all-or-none subunit interactions mediate slow deactivation of human ether-à-go-go-related gene K+ channels Effects of outer mouth mutations on hERG channel function: a comparison with similar mutations in the Shaker channel.Acceleration of P/C-type inactivation in voltage-gated K(+) channels by methionine oxidation.Carboxyl tail prevents yeast K(+) channel closure: proposal of an integrated model of TOK1 gating Tuning FlaSh: redesign of the dynamics, voltage range, and color of the genetically encoded optical sensor of membrane potential.The link between ion permeation and inactivation gating of Kv4 potassium channels.A physical model of potassium channel activation: from energy landscape to gating kinetics Slow inactivation in voltage gated potassium channels is insensitive to the binding of pore occluding peptide toxins.A self-consistent approach for determining pairwise interactions that underlie channel activation.The cooperative voltage sensor motion that gates a potassium channel.A multipoint hydrogen-bond network underlying KcsA C-type inactivation.Inter-subunit interactions across the upper voltage sensing-pore domain interface contribute to the concerted pore opening transition of Kv channels.Status of the intracellular gate in the activated-not-open state of shaker K+ channels Gating transitions in the selectivity filter region of a sodium channel are coupled to the domain IV voltage sensor.Modulation of Closed-State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4-AP Induced Potentiation.Initial steps in the opening of a Shaker potassium channel.An S6 mutation in BK channels reveals beta1 subunit effects on intrinsic and voltage-dependent gating Molecular mechanism for depolarization-induced modulation of Kv channel closure.Ion-binding properties of a K+ channel selectivity filter in different conformations.Fast inactivation in Shaker K+ channels. Properties of ionic and gating currents.Voltage-dependent structural interactions in the Shaker K(+) channel.A conducting state with properties of a slow inactivated state in a shaker K(+) channel mutant.Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation.Macroscopic Na+ currents in the "Nonconducting" Shaker potassium channel mutant W434F.Protein rearrangements underlying slow inactivation of the Shaker K+ channel.Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels.Molecular coupling of S4 to a K(+) channel's slow inactivation gate Can Shaker potassium channels be locked in the deactivated state?

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P2860

How does the W434F mutation block current in Shaker potassium channels?

http://www.wikidata.org/entity/Q36411800

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1997 nî lūn-bûn

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年學術文章

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1997年學術文章

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1997年學術文章

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name

How does the W434F mutation block current in Shaker potassium channels?

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How does the W434F mutation block current in Shaker potassium channels?

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How does the W434F mutation block current in Shaker potassium channels?

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How does the W434F mutation block current in Shaker potassium channels?

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prefLabel

How does the W434F mutation block current in Shaker potassium channels?

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How does the W434F mutation block current in Shaker potassium channels?

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The Journal of General Physiology

P1476

How does the W434F mutation block current in Shaker potassium channels?

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P2093

F J Sigworth

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

Y Yan

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

Y Yang

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

P2860

Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila

Biophysical and molecular mechanisms of Shaker potassium channel inactivation

Silver as a probe of pore-forming residues in a potassium channel.

Data transformations for improved display and fitting of single-channel dwell time histograms

Recovery from C-type inactivation is modulated by extracellular potassium.

C-type inactivation of a voltage-gated K+ channel occurs by a cooperative mechanism

Cooperative subunit interactions in C-type inactivation of K channels.

A single nonpolar residue in the deep pore of related K+ channels acts as a K+:Rb+ conductance switch

Gating currents in Shaker K+ channels. Implications for activation and inactivation models

Tandem linkage of Shaker K+ channel subunits does not ensure the stoichiometry of expressed channels

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779-789

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scholarly article

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10.1085/JGP.109.6.779

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6

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