New Binding Site on Common Molecular Scaffold Provides HERG Channel Specificity of Scorpion Toxin BeKm-1-Reference-Cited by-同舟云学术

New Binding Site on Common Molecular Scaffold Provides HERG Channel Specificity of Scorpion Toxin BeKm-1

Published:2002-11 Issue:45 Volume:277 Page:43104-43109
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Korolkova Yuliya V.,Bocharov Eduard V.,Angelo Kamilla,Maslennikov Innokenty V.,Grinenko Olga V.,Lipkin Aleksey V.,Nosyreva Elena D.,Pluzhnikov Kirill A.,Olesen Søren-Peter,Arseniev Alexander S.,Grishin Eugene V.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. The charybdotoxin family of K+ channel-blocking peptides

2. A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies

3. Potassium channels: from scorpion venoms to high-resolution structure

4. Structural determinants of scorpion toxin affinity: The charybdotoxin (α-KTX) family of K+-channel blocking peptides

5. An ERG Channel Inhibitor from the Scorpion Buthus eupeus

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