The phosphorylation state of both hERG and KvLQT1 mediates protein-protein interactions between these complementary cardiac potassium channel alpha subunits-Reference-Cited by-同舟云学术

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The phosphorylation state of both hERG and KvLQT1 mediates protein-protein interactions between these complementary cardiac potassium channel alpha subunits

Published:2021-04 Issue:4 Volume:1863 Page:183556
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Popescu Medeea C.,Lee Yeon J.,Kim Stephanie S.,Wade Heidi M.,Papakyrikos Amanda M.,Darling Louise E.O.

Funder

Wellesley College

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference35 articles.

1. Molecular mechanisms of adrenergic stimulation in the heart;Sampson;Heart Rhythm.,2010

2. Sanguinetti, M.C., et al., Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. Nature, 1996. 384(6604): p. 80–3.

3. Barhanin, J., et al., K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current. Nature, 1996. 384(6604): p. 78–80.

4. MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia;Abbott;Cell,1999

5. Molecular pathophysiology of congenital long QT syndrome;Bohnen;Physiol. Rev.,2016

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