External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

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Role of Kir2.1 in human monocyte-derived foam cell maturation.Apoptosis of Corneal Epithelial Cells Caused by Ultraviolet B-induced Loss of K(+) is Inhibited by Ba(2.).L-Phosphinothricin modulation of inwardly rectifying K(+) channels increased excitability in striatal medium-sized spiny neurons.

P2860

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P2860

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

Item

http://www.wikidata.org/entity/Q43504598

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh-hant

name

External Ba

@nl

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

@en

type

Item

label

External Ba

@nl

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

@en

prefLabel

External Ba

@nl

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

@en

P1476

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

@en

P2093

David Fedida

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

Zhuren Wang

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

P2860

Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits

Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors

The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium

Electrophysiological and pharmacological correspondence between Kv4.2 current and rat cardiac transient outward current

Regulation of dendritic excitability by activity-dependent trafficking of the A-type K+ channel subunit Kv4.2 in hippocampal neurons

The barium site in a potassium channel by x-ray crystallography.

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 permanent ion binding site located between two gates of the Shaker K+ channel.

Potassium blocks barium permeation through a calcium-activated potassium channel.

P304

C370-81

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

P31

scholarly article

P356

10.1152/AJPCELL.00267.2012

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

P433

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

P478

304

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

P50

Steven J Kehl

P577

2012-12-12T00:00:00Z

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

P5875

233930634

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

P698

23242186

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

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

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P2860

P2860

External Ba(2+) block of Kv4.2 channels is enhanced in the closed-inactivated state.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698