(Q28215695)

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Molecular identification and characterisation of the human eag2 potassium channel

scientific article (publication date: 31 July 2002)

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Molecular identification and characterisation of the human eag2 potassium channel (English)

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author name string

M Ju

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1

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D Wray

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2

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language of work or name

English

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publication date

31 July 2002

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published in

FEBS Letters

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volume

524

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issue

1-3

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page(s)

204-10

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cites work

Physiology of EAG K+ channels

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7 January 2021

Cloning of components of a novel subthreshold-activating K(+) channel with a unique pattern of expression in the cerebral cortex.

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7 January 2021

Cloning and functional expression of rat eag2, a new member of the ether-à-go-go family of potassium channels and comparison of its distribution with that of eag1.

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Cloning of a human ether-a-go-go potassium channel expressed in myoblasts at the onset of fusion

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Local movement in the S2 region of the voltage-gated potassium channel hKv2.1 studied using cysteine mutagenesis

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Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain

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Analysis of the cyclic nucleotide binding domain of the HERG potassium channel and interactions with KCNE2

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Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-à-go-go potassium channel

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Inhibition of human ether à go-go potassium channels by Ca(2+)/calmodulin

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Elevation of intracellular calcium by muscarinic receptor activation induces a block of voltage-activated rat ether-à-go-go channels in a stably transfected cell line

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A K+ channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current.

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Oncogenic potential of EAG K(+) channels

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7 January 2021

Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.

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Amino terminal-dependent gating of the potassium channel rat eag is compensated by a mutation in the S4 segment

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A structural basis for drug-induced long QT syndrome

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An amino acid residue whose change by mutation affects drug binding to the HERG channel

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Cytoskeletal interactions determine the electrophysiological properties of human EAG potassium channels.

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Functional distinction of human EAG1 and EAG2 potassium channels

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Molecular determinants of inactivation and dofetilide block in ether a-go-go (EAG) channels and EAG-related K(+) channels

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10.1016/S0014-5793(02)03055-7

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4891460

OpenCitations bibliographic resource ID

4891460

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4891460

(Q28215695)

Molecular identification and characterisation of the human eag2 potassium channel

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