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  Different relevance of inactivation and F468 residue in the mechanisms of hEag1 channel blockage by astemizole, imipramine and dofetilide

Gómez-Varela, D., Contreras-Jurado, C., Furini, S., García-Ferreiro, R., Stühmer, W., & Pardo, L. A. (2006). Different relevance of inactivation and F468 residue in the mechanisms of hEag1 channel blockage by astemizole, imipramine and dofetilide. FEBS Letters, 580(21), 5059-5066.

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Gómez-Varela, David, Author
Contreras-Jurado, Constanza1, Author              
Furini, Simone1, Author              
García-Ferreiro, Rafael1, Author              
Stühmer, Walter1, Author              
Pardo, Luis A.1, Author              
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1Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173656              

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Free keywords: two-electrode voltage clamp; Xenopus oocytes; Ether a go-go; potassium channels; mutagenesis; docking HERG POTASSIUM CHANNELS; LONG QT SYNDROME; K+ CHANNEL; MOLECULAR DETERMINANTS; BINDING-SITE; XENOPUS OOCYTES; EAG CHANNELS; ETHER; PROTEINS; AFFINITY
 Abstract: The relevance of a point mutation at the C-terminal end of the S6 helix (F468) and the introduction of C-type inactivation in the blockage of hEag1 channels by astemizole, imipramine and dofetilide was tested. C-type inactivation decreased block by asternizole and dofetilide but not imipramine, suggesting different binding sites in the channel. F468C mutation increased IC50 for asternizole and imipramine but in contrast to HERG channels, only slightly for dofetilide. Together with measurements on recovery of blocking, our observations indicate that the mechanism of hEag1 blockage by each of these drugs is different, and suggest relevant structural differences between hEag1 and HERG channels. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2006-09
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 292152
ISI: 000240693200014
ISI: 000240693200014
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Title: FEBS Letters
  Alternative Title : FEBS Lett.
Source Genre: Journal
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Pages: - Volume / Issue: 580 (21) Sequence Number: - Start / End Page: 5059 - 5066 Identifier: ISSN: 0014-5793