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10.1016/j.isci.2021.102370 http://scihub22266oqcxt.onion/10.1016/j.isci.2021.102370 33912817!8066426!33912817     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       iScience 2021 ; 24 (4): 102370 Nephropedia Template TP {{tp|p=33912817|t=2021. Identification and mechanistic analysis of an inhibitor of the CorC Mg(2+) transporter |pdf=|usr=}}{{33912817}} gab.com Text Identification and mechanistic analysis of an inhibitor of the CorC Mg(2+) transporter JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=33912817 #FOAvip The CorC/CNNM family of Na(+)-dependent Mg(2+) transporters is ubiquitously conserved from bacteria to humans. CorC, the bacterial CorC/CNNM family of proteins, is involved in resistance to antibiotic exposure and in the survival of pathogenic microorganisms in their host environment. The CorC/CNNM family proteins possess a cytoplasmic region containing the regulatory ATP-binding site. CorC and CNNM have attracted interest as therapeutic targets, whereas inhibitors targeting the ATP-binding site have not been identified. Here, we performed a virtual screening of CorC by targeting its ATP-binding site, identified a compound named IGN95a with inhibitory effects on ATP binding and Mg(2+) export, and determined the cytoplasmic domain structure in complex with IGN95a. Furthermore, a chemical cross-linking experiment indicated that with ATP bound to the cytoplasmic domain, the conformational equilibrium of CorC was shifted more toward the inward-facing state of the transmembrane domain. In contrast, IGN95a did not induce such a shift. Twit Text FOAVip Identification and mechanistic analysis of an inhibitor of the CorC Mg(2+) transporter ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=33912817 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33912817 #FOAvip English Wikipedia <ref>{{Cite pmid|33912817}}</ref> Identification and mechanistic analysis of an inhibitor of the CorC Mg(2+) transporter #MMPMID33912817 Huang Y; Mu K; Teng X; Zhao Y; Funato Y; Miki H; Zhu W; Xu Z; Hattori M iScience 2021[Apr]; 24 (4): 102370 PMID33912817show ga The CorC/CNNM family of Na(+)-dependent Mg(2+) transporters is ubiquitously conserved from bacteria to humans. CorC, the bacterial CorC/CNNM family of proteins, is involved in resistance to antibiotic exposure and in the survival of pathogenic microorganisms in their host environment. The CorC/CNNM family proteins possess a cytoplasmic region containing the regulatory ATP-binding site. CorC and CNNM have attracted interest as therapeutic targets, whereas inhibitors targeting the ATP-binding site have not been identified. Here, we performed a virtual screening of CorC by targeting its ATP-binding site, identified a compound named IGN95a with inhibitory effects on ATP binding and Mg(2+) export, and determined the cytoplasmic domain structure in complex with IGN95a. Furthermore, a chemical cross-linking experiment indicated that with ATP bound to the cytoplasmic domain, the conformational equilibrium of CorC was shifted more toward the inward-facing state of the transmembrane domain. In contrast, IGN95a did not induce such a shift. äIdentification and mechanistic analysis of an inhibitor of the CorC Mg(epmc).pdf DeepDyve Pubget Overpricing