Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain-Reference-Cited by-同舟云学术

Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain

Published:2018-09-03 Issue:19 Volume:596 Page:4629-4650
ISSN:0022-3751
Container-title:The Journal of Physiology
language:en
Short-container-title:J Physiol

Author:

Kume Shinichiro¹²³,Shimomura Takushi¹²,Tateyama Michihiro¹²,Kubo Yoshihiro¹²^ORCID

Affiliation:

1. Division of Biophysics and Neurobiology; Department of Molecular and Cellular Physiology; National Institute for Physiological Sciences; Okazaki Japan

2. Department of Physiological Sciences; School of Life Science; SOKENDAI Hayama Japan

3. Present address: Department of Pathophysiology; Oita University School of Medicine; Yufu Oita Japan

Funder

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Physiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1113/JP276208/fullpdf

Reference50 articles.

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2. Role of intracellular domains in the function of the herg potassium channel;Al-Owais;Eur Biophys J,2009

3. Structure of the carboxy-terminal region of a KCNH channel;Brelidze;Nature,2012

4. Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods;Brelidze;J Biol Chem,2009

5. Structure of the C-terminal region of an ERG channel and functional implications;Brelidze;Proc Natl Acad Sci U S A,2013

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4. Investigation of PAS and CNBH domain interactions in hERG channels and effects of long-QT syndrome-causing mutations with surface plasmon resonance;Journal of Biological Chemistry;2022-01

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