Gating and regulation of KCNH (ERG, EAG, and ELK) channels by intracellular domains
Author:
Affiliation:
1. Department of Physiology, University of Maryland School of Medicine, Baltimore, MD, USA
Funder
NIH/NIGMS
Publisher
Informa UK Limited
Subject
Biochemistry,Biophysics
Link
https://www.tandfonline.com/doi/pdf/10.1080/19336950.2020.1816107
Reference95 articles.
1. The hERG potassium channel intrinsic ligand regulates N- and C-terminal interactions and channel closure
2. Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain
3. Chlorpromazine binding to the PAS domains uncovers the effect of ligand modulation on EAG channel activity
4. Structure of KCNH2 cyclic nucleotide-binding homology domain reveals a functionally vital salt-bridge
5. A family of potassium channel genes related to eag in Drosophila and mammals.
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1. Revealing a hidden conducting state by manipulating the intracellular domains in KV10.1 exposes the coupling between two gating mechanisms;eLife;2024-09-11
2. Finely ordered intracellular domain harbors an allosteric site to modulate physiopathological function of P2X3 receptors;Nature Communications;2024-09-03
3. Revealing a hidden conducting state by manipulating the intracellular domains in KV10.1 exposes the coupling between two gating mechanisms;2024-08-20
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