The mutation L69P in the PAS domain of the hERG potassium channel results in LQTS by trafficking deficiency-Reference-Cited by-同舟云学术

The mutation L69P in the PAS domain of the hERG potassium channel results in LQTS by trafficking deficiency

Published:2020-01-01 Issue:1 Volume:14 Page:163-174
ISSN:1933-6950
Container-title:Channels
language:en
Short-container-title:Channels

Author:

Jenewein Tina¹,Kanner Scott A.²^ORCID,Bauer Daniel³^ORCID,Hertel Brigitte⁴,Colecraft Henry M.²^ORCID,Moroni Anna⁵^ORCID,Thiel Gerhard⁴^ORCID,Kauferstein Silke¹^ORCID

Affiliation:

1. Institute of Legal Medicine, University of Frankfurt, Frankfurt Am Main, Germany

2. Department of Physiology and Cellular Biophysics, College of Physicians and Surgeons, Columbia University, New York, NY, USA

3. Computational Biology and Simulation Group, Department of Biology, Technische Universita ̈t Darmstadt, Darmstadt, Germany

4. Department of Biology, Technische Universität Darmstadt, Darmstadt, Germany

5. Department of Biosciences and CNR IBF-Mi, University of Milano, Milano, Italy

Funder

FP7 Ideas: European Research Council

Publisher

Informa UK Limited

Subject

Biochemistry,Biophysics

Link

https://www.tandfonline.com/doi/pdf/10.1080/19336950.2020.1751522

Reference35 articles.

1. A mechanistic link between an inherited and an acquird cardiac arrthytmia: HERG encodes the IKr potassium channel

2. HERG, a Human Inward Rectifier in the Voltage-Gated Potassium Channel Family

3. hERG K+Channels: Structure, Function, and Clinical Significance

4. Cryo-EM Structure of the Open Human Ether-à-go-go -Related K + Channel hERG

5. Crystal Structure and Functional Analysis of the HERG Potassium Channel N Terminus

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2. Role and mechanism of chaperones calreticulin and ERP57 in restoring trafficking to mutant HERG‑A561V protein;International Journal of Molecular Medicine;2021-07-01