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10.1038/srep21493 http://scihub22266oqcxt.onion/10.1038/srep21493 26869275!4751470!26869275     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2016 ; 6 (ä): 21493 Nephropedia Template TP {{tp|p=26869275|t=2016. A synergistic blocking effect of Mg(2)(+) and spermine on the inward rectifier K(+) (Kir2 1) channel pore |pdf=|usr=}}{{26869275}} gab.com Text A synergistic blocking effect of Mg(2)(+) and spermine on the inward rectifier K(+) (Kir2 1) channel pore JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26869275 #FOAvip Inward rectifier K(+) channels (Kir2.1) exhibit an extraordinary rectifying feature in the current-voltage relationship. We have previously showed that the bundle-crossing region of the transmembrane domain constitutes the crucial segment responsible for the polyamine block. In this study, we demonstrated that the major blocking effect of intracellular Mg(2+) on Kir2.1 channels is also closely correlated with K(+) current flow, and the coupled movements of Mg(2+) and K(+) seem to happen in the same flux-coupling segment of the pore as polyamines. With a preponderant outward K(+) flow, intracellular Mg(2+) would also be pushed to and thus stay at the outermost site of a flux-coupling segment in the bundle-crossing region of Kir2.1 channels to block the pore, although with a much lower apparent affinity than spermine (SPM). However, in contrast to the evident possibilities of outward exit of SPM through the channel pore especially during strong membrane depolarization, intracellular Mg(2+) does not seem to traverse the Kir2.1 channel pore in any case. Intracellular Mg(2+) and SPM therefore may have a synergistic action on the pore-blocking effect, presumably via prohibition of the outward exit of the higher-affinity blocking SPM by the lower-affinity Mg(2+). Twit Text FOAVip A synergistic blocking effect of Mg(2)(+) and spermine on the inward rectifier K(+) (Kir2 1) channel pore ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26869275 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26869275 #FOAvip English Wikipedia <ref>{{Cite pmid|26869275}}</ref> A synergistic blocking effect of Mg(2)(+) and spermine on the inward rectifier K(+) (Kir2 1) channel pore #MMPMID26869275 Huang CW; Kuo CC Sci Rep 2016[Feb]; 6 (ä): 21493 PMID26869275show ga Inward rectifier K(+) channels (Kir2.1) exhibit an extraordinary rectifying feature in the current-voltage relationship. We have previously showed that the bundle-crossing region of the transmembrane domain constitutes the crucial segment responsible for the polyamine block. In this study, we demonstrated that the major blocking effect of intracellular Mg(2+) on Kir2.1 channels is also closely correlated with K(+) current flow, and the coupled movements of Mg(2+) and K(+) seem to happen in the same flux-coupling segment of the pore as polyamines. With a preponderant outward K(+) flow, intracellular Mg(2+) would also be pushed to and thus stay at the outermost site of a flux-coupling segment in the bundle-crossing region of Kir2.1 channels to block the pore, although with a much lower apparent affinity than spermine (SPM). However, in contrast to the evident possibilities of outward exit of SPM through the channel pore especially during strong membrane depolarization, intracellular Mg(2+) does not seem to traverse the Kir2.1 channel pore in any case. Intracellular Mg(2+) and SPM therefore may have a synergistic action on the pore-blocking effect, presumably via prohibition of the outward exit of the higher-affinity blocking SPM by the lower-affinity Mg(2+). |Animals[MESH] |Ion Transport/physiology[MESH] |Magnesium/agonists/*metabolism[MESH] |Mice[MESH] |Potassium Channel Blockers/*metabolism[MESH] |Potassium Channels, Inwardly Rectifying/*antagonists & inhibitors/*metabolism[MESH] |Spermine/agonists/*metabolism[MESH]A synergistic blocking effect of Mg(2)(+) and spermine on the inward r(epmc).pdf DeepDyve Pubget Overpricing