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10.1073/pnas.1604082113 http://scihub22266oqcxt.onion/10.1073/pnas.1604082113 C5056077!5056077!27647906     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 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 (40): E5962-71 Nephropedia Template TP {{tp|p=27647906|t=2016. Molecular mechanism of Zn2+ inhibition of a voltage-gated proton channel |pdf=|usr=}}{{27647906}} gab.com Text Molecular mechanism of Zn2+ inhibition of a voltage-gated proton channel JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27647906 #FOAvip Zn2+ inhibition of voltage-gated proton (Hv1) channels has important physiological roles, such as quiescence of sperm in the male reproductive system. Here, we show that Zn2+ binds to different states of Hv1, and we propose a possible mechanism for Zn2+ inhibition of Hv1. Several residues are found to be involved in Zn2+ binding, and we provide detailed information about how these residues contribute to the functional effect of Zn2+ binding. This study provides valuable information for future drug development for Hv1 channels. Twit Text FOAVip Molecular mechanism of Zn2+ inhibition of a voltage-gated proton channel ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27647906 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27647906 #FOAvip English Wikipedia <ref>{{Cite pmid|27647906}}</ref> Molecular mechanism of Zn2+ inhibition of a voltage-gated proton channel #MMPMID27647906 Qiu F; Chamberlin A; Watkins BM; Ionescu A; Perez ME; Barro-Soria R; González C; Noskov SY; Larsson HP Proc Natl Acad Sci U S A 2016[Oct]; 113 (40): E5962-71 PMID27647906show ga Zn2+ inhibition of voltage-gated proton (Hv1) channels has important physiological roles, such as quiescence of sperm in the male reproductive system. Here, we show that Zn2+ binds to different states of Hv1, and we propose a possible mechanism for Zn2+ inhibition of Hv1. Several residues are found to be involved in Zn2+ binding, and we provide detailed information about how these residues contribute to the functional effect of Zn2+ binding. This study provides valuable information for future drug development for Hv1 channels. äMolecular mechanism of Zn2+ inhibition of a voltage-gated proton chann(epmc).pdf DeepDyve Pubget Overpricing