A carboxy‐terminal domain determines the subunit specificity of KCNQ K + channel assembly-Reference-Cited by-同舟云学术

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A carboxy‐terminal domain determines the subunit specificity of KCNQ K + channel assembly

Published:2003-01 Issue:1 Volume:4 Page:76-81
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Schwake Michael¹²,Jentsch Thomas J¹,Friedrich Thomas³

Affiliation:

1. Centre for Molecular Neurobiology Hamburg, ZMNH Falkenried 94 D‐20251 Hamburg Germany

2. Present address: Institute of Biochemistry, Christian Albrechts University Kiel Olshausenstrasse 40 D‐24098 Kiel Germany

3. Max Planck Institute of Biophysics Kennedyallee 70 D‐60596 Frankfurt Germany

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1038/sj.embor.embor715

Reference27 articles.

1. KvLQT1 and IsK (minK) proteins associate to form the IKS cardiac potassium current

2. A Potassium Channel Mutation in Neonatal Human Epilepsy

3. A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family

4. Novel mutations in KvLQT1 that affect Iks activation through interactions with Isk

5. Neuronal KCNQ potassium channels:physislogy and role in disease

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1. Polymodal K+ channel modulation contributes to dual analgesic and anti-inflammatory actions of traditional botanical medicines;Communications Biology;2024-08-28

2. A versatile functional interaction between electrically silent KV subunits and KV7 potassium channels;Cellular and Molecular Life Sciences;2024-07-14

3. G protein βγ regulation of KCNQ-encoded voltage-dependent K channels;Frontiers in Physiology;2024-04-09

4. Electrophysiological signatures of a developmental delay in a stem cell model ofKCNQ2developmental and epileptic encephalopathy;2024-03-13

5. A Versatile Functional Interaction between Electrically Silent K_VSubunits and K_V7 Potassium Channels;2024-02-27

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