Electrophysiological characterization of the modified hERG T potassium channel used to obtain the first cryo‐EM hERG structure
Author:
Affiliation:
1. School of Physiology and Pharmacology and Neuroscience Biomedical Sciences Building The University of BristolUniversity Walk Bristol UK
2. School of Biochemistry Biomedical Sciences Building The University of BristolUniversity Walk Bristol UK
Funder
British Heart Foundation
Publisher
Wiley
Subject
Physiology (medical),Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.14814/phy2.14568
Reference54 articles.
1. Large-scale mutational analysis of Kv11.1 reveals molecular insights into type 2 long QT syndrome
2. An Update on the Structure of hERG;Butler A.;Front Pharmacol,2020
3. Action potential clamp characterization of the S631A hERG mutation associated with short QT syndrome
4. Functional and pharmacological characterization of an S5 domain hERG mutation associated with short QT syndrome
5. The molecular determinants of R-roscovitine block of hERG channels
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3. A need for exhaustive and standardized characterization of ion channels activity. The case of KV11.1;Frontiers in Physiology;2023-02-13
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