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10.1073/pnas.1610414114 http://scihub22266oqcxt.onion/10.1073/pnas.1610414114 C5358401!5358401!28235784     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11): E2156-65 Nephropedia Template TP {{tp|p=28235784|t=2017. Localization of the gate and selectivity filter of the full-length P2X7 receptor |pdf=|usr=}}{{28235784}} gab.com Text Localization of the gate and selectivity filter of the full-length P2X7 receptor JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28235784 #FOAvip The P2X7 receptor (P2X7R) was the first ion channel that was suggested to transform from cation selective into nonselective by undergoing a dilatation in the diameter of its transmembrane pathway following sustained activation. This change requires that the selectivity filter behave as a dynamic structure. Here, we used a single-channel analysis of cysteine substitution mutants to find that the gate and selectivity filter of P2X7R are colocalized and primarily determined by one single residue, S342. We found the agonist-opened selectivity filter to be completely stable over time, indicating that use-dependent dilatation of the channel diameter does not occur. Instead, P2X7R exhibits striking susceptibility to remain in the open state for longer when the channel pore contains slowly or nonpermeating cations. Twit Text FOAVip Localization of the gate and selectivity filter of the full-length P2X7 receptor ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28235784 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28235784 #FOAvip English Wikipedia <ref>{{Cite pmid|28235784}}</ref> Localization of the gate and selectivity filter of the full-length P2X7 receptor #MMPMID28235784 Pippel A; Stolz M; Woltersdorf R; Kless A; Schmalzing G; Markwardt F Proc Natl Acad Sci U S A 2017[Mar]; 114 (11): E2156-65 PMID28235784show ga The P2X7 receptor (P2X7R) was the first ion channel that was suggested to transform from cation selective into nonselective by undergoing a dilatation in the diameter of its transmembrane pathway following sustained activation. This change requires that the selectivity filter behave as a dynamic structure. Here, we used a single-channel analysis of cysteine substitution mutants to find that the gate and selectivity filter of P2X7R are colocalized and primarily determined by one single residue, S342. We found the agonist-opened selectivity filter to be completely stable over time, indicating that use-dependent dilatation of the channel diameter does not occur. Instead, P2X7R exhibits striking susceptibility to remain in the open state for longer when the channel pore contains slowly or nonpermeating cations. äLocalization of the gate and selectivity filter of the full-length P2X(epmc).pdf DeepDyve Pubget Overpricing