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10.1085/jgp.201611616 http://scihub22266oqcxt.onion/10.1085/jgp.201611616 C5004336!5004336!27527100     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Gen+Physiol 2016 ; 148 (3): 227-37 Nephropedia Template TP {{tp|p=27527100|t=2016. Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids |pdf=|usr=}}{{27527100}} gab.com Text Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids JO: J Gen Physiol http://www.kidney.de/pget.php?&tw=1&pmid=27527100 #FOAvip Phospholipids are required to bind to two distinct sites on the inward rectifier potassium channel for maximal efficacy. Lee et al. show that a membrane-associating tryptophan residue in the second site can mimic the effect of phospholipid binding and cause a conformational change to reveal the primary binding site. Twit Text FOAVip Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids ????J Gen Physiol http://www.kidney.de/pget.php?&tw=1&pmid=27527100 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27527100 #FOAvip English Wikipedia <ref>{{Cite pmid|27527100}}</ref> Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids #MMPMID27527100 Lee SJ; Ren F; Zangerl-Plessl EM; Heyman S; Stary-Weinzinger A; Yuan P; Nichols CG J Gen Physiol 2016[Sep]; 148 (3): 227-37 PMID27527100show ga Phospholipids are required to bind to two distinct sites on the inward rectifier potassium channel for maximal efficacy. Lee et al. show that a membrane-associating tryptophan residue in the second site can mimic the effect of phospholipid binding and cause a conformational change to reveal the primary binding site. äStructural basis of control of inward rectifier Kir2 channel gating by(epmc).pdf DeepDyve Pubget Overpricing