Výsledky vyhledávání - "Tandem pore domain potassium channel"

Structural modeling of human cardiac sodium channel pore domain

Autor: Yi Xiao, Shiyong Liu, Xiaofeng Ji

The pore domain of human voltage-dependent cardiac sodium channel Nav1.5 (hNav1.5) is the crucial binding targets for anti-arrhythmics drugs and some local anesthetic drugs but its three-dimensional structure is still lacking. This has affected the d

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The voltage-sensing domain of a phosphatase gates the pore of a potassium channel

Autor: Indra Schroeder, Gerhard Thiel, James L. Van Etten, Cristina Arrigoni, Giulia Romani, Anna Moroni

Publikováno v: The Journal of General Physiology
The journal of general physiology (Online) 141 (2013): 389–395. doi:10.1085/jgp.201210940
info:cnr-pdr/source/autori:Cristina Arrigoni, Indra Schroeder, Giulia Romani, James L. Van Etten, Gerhard Thiel, and Anna Moroni/titolo:The voltage-sensing domain of a phosphatase gates the pore of a potassium channel/doi:10.1085%2Fjgp.201210940/rivista:The journal of general physiology (Online)/anno:2013/pagina_da:389/pagina_a:395/intervallo_pagine:389–395/volume:141

The modular architecture of voltage-gated K+ (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channe

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http://europepmc.org/articles/PMC3581695

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KCNK10, a tandem pore domain potassium channel, is a regulator of mitotic clonal expansion during the early stage of adipocyte differentiation

Autor: Mami Asano, Masayoshi Imagawa, Shigehiro Osada, Makoto Nishizuka, Takahiro Hayashi

Publikováno v: International Journal of Molecular Sciences
Volume 15
Issue 12
Pages 22743-22756
International Journal of Molecular Sciences, Vol 15, Iss 12, Pp 22743-22756 (2014)

KCNK10, a member of tandem pore domain potassium channel family, gives rise to leak K+ currents. It plays important roles in stabilizing the negative resting membrane potential and in counterbalancing depolarization. We previously demonstrated that k

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https://pubmed.ncbi.nlm.nih.gov/25501330

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A unique alkaline pH-regulated and fatty acid-activated tandem pore domain potassium channel (K2P) from a marine sponge

Autor: Sally P. Leys, Qiong-Yao Tang, Robert Heler, Gregory D. Wells, Erica N. Pritchard, Diomedes E. Logothetis, Linda M. Boland, Gabrielle J. Tompkins-MacDonald

Publikováno v: Journal of Experimental Biology. 215:2435-2444

SUMMARY A cDNA encoding a potassium channel of the two-pore domain family (K2P, KCNK) of leak channels was cloned from the marine sponge Amphimedon queenslandica. Phylogenetic analysis indicated that AquK2P cannot be placed into any of the establishe

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https://doi.org/10.1242/jeb.066233

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Coupling between the voltage-sensing and pore domains in a voltage-gated potassium channel

Autor: Stephen H. White, Eric V. Schow, Alex Nizkorodov, Douglas J. Tobias, J. Alfredo Freites

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818:1726-1736

article i nfo Voltage-dependent potassium (Kv), sodium (Nav), and calcium channels open and close in response to changes in transmembrane (TM) potential, thus regulating cell excitability by controlling ion flow across the membrane. An outstanding qu

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https://doi.org/10.1016/j.bbamem.2012.02.029

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Biogenesis of the pore architecture of a voltage-gated potassium channel

Autor: Alper Dagcan, Benoît Roux, Christine Gajewski, Carol Deutsch

Publikováno v: Proceedings of the National Academy of Sciences. 108:3240-3245

The pore domain of voltage-gated potassium (Kv) channels consists of transmembrane helices S5 and S6, the turret, the pore helix, the selectivity filter, and the loop preceding S6, with a tertiary reentrant structure between S5 and S6. Using biogenic

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https://doi.org/10.1073/pnas.1017097108

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Novel neuroprotectant chiral 3-n-butylphthalide inhibits tandem-pore-domain potassium channel TREK-1

Autor: Qiao-qiao Shi, Xiaoliang Wang, Dong-xu Cao, Xin-cai Ji, Wanhong Zhao

Publikováno v: Acta Pharmacologica Sinica. 32:182-187

To study the effects of 3-n-butylphthalide (NBP) on the TREK-1 channel expressed in Chinese hamster ovary (CHO) cells. Whole-cell patch-clamp recording was used to record TREK-1 channel currents. The effects of varying doses of l-NBP on TREK-1 curren

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76ac58aea69a3bc1fa2f2b994e4c0700
https://doi.org/10.1038/aps.2010.210

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Pore opening and closing of a pentameric ligand-gated ion channel

Autor: Fangqiang Zhu, Gerhard Hummer

Publikováno v: Proceedings of the National Academy of Sciences. 107:19814-19819

Nerve signaling in humans and chemical sensing in bacteria both rely on the controlled opening and closing of the ion-conducting pore in pentameric ligand-gated ion channels. With the help of a multiscale simulation approach that combines mixed elast

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https://doi.org/10.1073/pnas.1009313107

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Potassium Channel Block by a Tripartite Complex of Two Cationophilic Ligands and a Potassium Ion

Autor: Bojan Garic, Cedrick Mahieux, Boris S. Zhorov, Silke B. Bodendiek, Pavel I. Zimin, Heike Wulff

Publikováno v: Molecular Pharmacology. 78:588-599

Voltage-gated potassium channels (Kv) are targets for drugs of large chemical diversity. Although hydrophobic cations block Kv channels with Hill coefficients of 1, uncharged electron-rich (cationophilic) molecules often display Hill coefficients of

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https://doi.org/10.1124/mol.110.064014

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The Membrane-Bound State of K2P Potassium Channels

Autor: Werner Treptow, Michael L. Klein

Publikováno v: Journal of the American Chemical Society. 132:8145-8151

Potassium channel subunits composed of two-pore domains arranged in tandem (K(2P)) are of paramount importance for neural function. A variety of stimuli, such as membrane depolarization and tension, acidification, and anesthetic action, activate K(2P

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd383ba2e60e7bd7eb5a0537d5f60020
https://doi.org/10.1021/ja102191s

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