Looking over Toxin–K+ Channel Interactions. Clues from the Structural and Functional Characterization of α-KTx Toxin Tc32, a Kv1.3 Channel Blocker-Reference-Cited by-同舟云学术

Looking over Toxin–K+ Channel Interactions. Clues from the Structural and Functional Characterization of α-KTx Toxin Tc32, a Kv1.3 Channel Blocker

Published:2012-02-27 Issue:9 Volume:51 Page:1885-1894
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stehling Eliana G.¹,Sforça Mauricio L.²,Zanchin Nilson I. T.²,Oyama Sérgio²,Pignatelli Angela³,Belluzzi Ottorino³,Polverini Eugenia⁴,Corsini Romina⁵,Spisni Alberto⁵,Pertinhez Thelma A.⁵

Affiliation:

1. Department of Toxicological and Bromatologic Clinical Analyses, Faculty of Pharmaceutical Sciences of Ribeirão Preto, USP, Ribeirão Preto, Brazil

2. National Laboratory of Biosciences, Campinas, Brazil

3. Physiology and Biophysics Unit, Department of Biology and Evolution, University of Ferrara, Ferrara, Italy

4. Department of Physics, University of Parma, Parma, Italy

5. Chemistry and Structural Biochemistry Unit, Department of Experimental Medicine, University of Parma, Parma, Italy

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201713z

Reference56 articles.

1. Current views on scorpion toxins specific for K+-channels

2. Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR

3. Animal Toxins Acting on Voltage-Gated Potassium Channels

4. The functional dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels

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