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10.1073/pnas.1609964114 http://scihub22266oqcxt.onion/10.1073/pnas.1609964114 C5206518!5206518!27956641     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (52): E8359-68 Nephropedia Template TP {{tp|p=27956641|t=2016. On the role of water density fluctuations in the inhibition of a proton channel |pdf=|usr=}}{{27956641}} gab.com Text On the role of water density fluctuations in the inhibition of a proton channel JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27956641 #FOAvip Hv1, a voltage-gated proton channel, is an emerging pharmacological target implicated in many pathological conditions, including cancer and ischemic brain damage. We used the recently published experimental structure of Hv1 to generate structural models of relevant conformational states. Thermodynamic analyses of pore waters shed light on the molecular underpinnings of Hv1 druggability. We exploit this information to suggest possible optimizations of known inhibitors and identify a potential binding site located at the exit of the proton path. The resulting molecular picture paves the way for the discovery of novel Hv1 inhibitors and outlines a general approach for identifying druggable binding sites in ion channels. Twit Text FOAVip On the role of water density fluctuations in the inhibition of a proton channel ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27956641 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27956641 #FOAvip English Wikipedia <ref>{{Cite pmid|27956641}}</ref> On the role of water density fluctuations in the inhibition of a proton channel #MMPMID27956641 Gianti E; Delemotte L; Klein ML; Carnevale V Proc Natl Acad Sci U S A 2016[Dec]; 113 (52): E8359-68 PMID27956641show ga Hv1, a voltage-gated proton channel, is an emerging pharmacological target implicated in many pathological conditions, including cancer and ischemic brain damage. We used the recently published experimental structure of Hv1 to generate structural models of relevant conformational states. Thermodynamic analyses of pore waters shed light on the molecular underpinnings of Hv1 druggability. We exploit this information to suggest possible optimizations of known inhibitors and identify a potential binding site located at the exit of the proton path. The resulting molecular picture paves the way for the discovery of novel Hv1 inhibitors and outlines a general approach for identifying druggable binding sites in ion channels. äOn the role of water density fluctuations in the inhibition of a proto(epmc).pdf DeepDyve Pubget Overpricing