Structure of KCNE1 and Implications for How It Modulates the KCNQ1 Potassium Channel-Reference-Cited by-同舟云学术

Structure of KCNE1 and Implications for How It Modulates the KCNQ1 Potassium Channel

Published:2008-07-09 Issue:31 Volume:47 Page:7999-8006
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kang Congbao¹,Tian Changlin¹,Sönnichsen Frank D.¹,Smith Jarrod A.¹,Meiler Jens¹,George Alfred L.¹,Vanoye Carlos G.¹,Kim Hak Jun¹,Sanders Charles R.¹

Affiliation:

1. Departments of Biochemistry, Pharmacology, Chemistry, and Medicine, Vanderbilt University, Nashville, Tennessee 37232, Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106, and Department of Chemistry, Christian Albrechts University, Kiel, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800875q

Reference50 articles.

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

2. The MinK-related peptides

3. Coassembly of KVLQT1 and minK (IsK) proteins to form cardiac IKS potassium channel

4. Molecular Mechanism and Functional Significance of the MinK Control of the KvLQT1 Channel Activity

5. Disease‐associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanism

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