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10.1007/s12551-012-0078-7 http://scihub22266oqcxt.onion/10.1007/s12551-012-0078-7 C5425705!5425705!28510176     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 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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2013 ; 5 (1): 1-9 Nephropedia Template TP {{tp|p=28510176|t=2013. Molecular mechanisms of acetylcholine receptor?lipid interactions: from model membranes to human biology |pdf=|usr=}}{{28510176}} gab.com Text Molecular mechanisms of acetylcholine receptor lipid interactions: from model membranes to human biology JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510176 #FOAvip Lipids are potent modulators of the Torpedo nicotinic acetylcholine receptor. Lipids influence nicotinic receptor function by allosteric mechanisms, stabilizing varying proportions of pre-existing resting, open, desensitized, and uncoupled conformations. Recent structures reveal that lipids could alter function by modulating transmembrane ?-helix/?-helix packing, which in turn could alter the conformation of the allosteric interface that links the agonist-binding and transmembrane pore domains?this interface is essential in the coupling of agonist binding to channel gating. We discuss potential mechanisms by which lipids stabilize different conformational states in the context of the hypothesis that lipid?nicotinic receptor interactions modulate receptor function at biological synapses. Twit Text FOAVip Molecular mechanisms of acetylcholine receptor lipid interactions: from model membranes to human biology ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510176 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28510176 #FOAvip English Wikipedia <ref>{{Cite pmid|28510176}}</ref> Molecular mechanisms of acetylcholine receptor?lipid interactions: from model membranes to human biology #MMPMID28510176 Baenziger JE; daCosta CJB Biophys Rev 2013[Mar]; 5 (1): 1-9 PMID28510176show ga Lipids are potent modulators of the Torpedo nicotinic acetylcholine receptor. Lipids influence nicotinic receptor function by allosteric mechanisms, stabilizing varying proportions of pre-existing resting, open, desensitized, and uncoupled conformations. Recent structures reveal that lipids could alter function by modulating transmembrane ?-helix/?-helix packing, which in turn could alter the conformation of the allosteric interface that links the agonist-binding and transmembrane pore domains?this interface is essential in the coupling of agonist binding to channel gating. We discuss potential mechanisms by which lipids stabilize different conformational states in the context of the hypothesis that lipid?nicotinic receptor interactions modulate receptor function at biological synapses. äMolecular mechanisms of acetylcholine receptor?lipid interactions: fro(epmc).pdf DeepDyve Pubget Overpricing