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Literature DB >> 24314074

A complex partnership: KCNQ1 and KCNE1.

Guiscard Seebohm¹.

Abstract

Entities: Gene

Mesh：

Substances：

Year: 2013 PMID： 24314074 PMCID： PMC3853315 DOI： 10.1016/j.bpj.2013.10.022

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

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14 in total

1. K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current.

Authors: J Barhanin; F Lesage; E Guillemare; M Fink; M Lazdunski; G Romey
Journal: Nature Date: 1996-11-07 Impact factor: 49.962

2. Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel.

Authors: M C Sanguinetti; M E Curran; A Zou; J Shen; P S Spector; D L Atkinson; M T Keating
Journal: Nature Date: 1996-11-07 Impact factor: 49.962

3. Voltage-dependent inactivation of the human K+ channel KvLQT1 is eliminated by association with minimal K+ channel (minK) subunits.

Authors: M Tristani-Firouzi; M C Sanguinetti
Journal: J Physiol Date: 1998-07-01 Impact factor: 5.182

4. Ancillary subunits and stimulation frequency determine the potency of chromanol 293B block of the KCNQ1 potassium channel.

Authors: Glenna C L Bett; Michael J Morales; Derek L Beahm; Michael E Duffey; Randall L Rasmusson
Journal: J Physiol Date: 2006-08-03 Impact factor: 5.182

5. Molecular impact of MinK on the enantiospecific block of I(Ks) by chromanols.

Authors: C Lerche; G Seebohm; C I Wagner; C R Scherer; L Dehmelt; I Abitbol; U Gerlach; J Brendel; B Attali; A E Busch
Journal: Br J Pharmacol Date: 2000-12 Impact factor: 8.739

6. Mutation of colocalized residues of the pore helix and transmembrane segments S5 and S6 disrupt deactivation and modify inactivation of KCNQ1 K+ channels.

Authors: Guiscard Seebohm; Peter Westenskow; Florian Lang; Michael C Sanguinetti
Journal: J Physiol Date: 2005-01-13 Impact factor: 5.182

7. Single-channel characteristics of wild-type IKs channels and channels formed with two minK mutants that cause long QT syndrome.

Authors: F Sesti; S A Goldstein
Journal: J Gen Physiol Date: 1998-12 Impact factor: 4.086

A complex partnership: KCNQ1 and KCNE1.

1. K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current.

2. Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel.

3. Voltage-dependent inactivation of the human K+ channel KvLQT1 is eliminated by association with minimal K+ channel (minK) subunits.

4. Ancillary subunits and stimulation frequency determine the potency of chromanol 293B block of the KCNQ1 potassium channel.

5. Molecular impact of MinK on the enantiospecific block of I(Ks) by chromanols.

6. Mutation of colocalized residues of the pore helix and transmembrane segments S5 and S6 disrupt deactivation and modify inactivation of KCNQ1 K+ channels.

7. Single-channel characteristics of wild-type IKs channels and channels formed with two minK mutants that cause long QT syndrome.

8. Increase of the single-channel conductance of KvLQT1 potassium channels induced by the association with minK.

9. Activation and inactivation of homomeric KvLQT1 potassium channels.

10. Tight coupling of rubidium conductance and inactivation in human KCNQ1 potassium channels.

1. Effects of protein-protein interactions and ligand binding on the ion permeation in KCNQ1 potassium channel.

Review 2. Chemical modulation of Kv7 potassium channels.