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10.1038/s41598-017-08144-1 http://scihub22266oqcxt.onion/10.1038/s41598-017-08144-1 C5562840!5562840 !28821869     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28821869 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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 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 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28821869 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2017 ; 7 (1 ): 8806 Nephropedia Template TP {{tp|p=28821869 |t=2017. TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg(2+) and Mg·ATP |pdf=|usr=}}{{28821869 }} gab.com Text TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg(2+) and Mg·ATP JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28821869 #FOAvip TRPM6 and its homologue TRPM7 are ?-kinase-coupled divalent cation-selective channels activated upon reduction of cytosolic levels of Mg(2+) and Mg·ATP. TRPM6 is vital for organismal Mg(2+) balance. However, mechanistically the cellular role and functional nonredundancy of TRPM6 remain incompletely understood. Comparative analysis of native currents in primary cells from TRPM6- versus TRPM7-deficient mice supported the concept that native TRPM6 primarily functions as a constituent of heteromeric TRPM6/7 channels. However, heterologous expression of the human TRPM6 protein engendered controversial results with respect to channel characteristics including its regulation by Mg(2+) and Mg·ATP. To resolve this issue, we cloned the mouse TRPM6 (mTRPM6) cDNA and compared its functional characteristics to mouse TRPM7 (mTRPM7) after heterologous expression. Notably, we observed that mTRPM6 and mTRPM7 differentially regulate properties of heteromeric mTRPM6/7 channels: In the presence of mTRPM7, the extreme sensitivity of functionally expressed homomeric mTRPM6 to Mg(2+) is tuned to higher concentrations, whereas mTRPM6 relieves mTRPM7 from the tight inhibition by Mg·ATP. Consequently, the association of mTRPM6 with mTRPM7 allows for high constitutive activity of mTRPM6/7 in the presence of physiological levels of Mg(2+) and Mg·ATP, thus laying the mechanistic foundation for constant vectorial Mg(2+) transport specifically into epithelial cells. Twit Text FOAVip TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg(2+) and Mg·ATP ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28821869 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28821869 #FOAvip English Wikipedia <ref>{{Cite pmid|28821869 }}</ref> TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg(2+) and Mg·ATP #MMPMID28821869 Ferioli S ; Zierler S ; Zaißerer J ; Schredelseker J ; Gudermann T ; Chubanov V Sci Rep 2017[Aug]; 7 (1 ): 8806 PMID28821869 show ga TRPM6 and its homologue TRPM7 are ?-kinase-coupled divalent cation-selective channels activated upon reduction of cytosolic levels of Mg(2+) and Mg·ATP. TRPM6 is vital for organismal Mg(2+) balance. However, mechanistically the cellular role and functional nonredundancy of TRPM6 remain incompletely understood. Comparative analysis of native currents in primary cells from TRPM6- versus TRPM7-deficient mice supported the concept that native TRPM6 primarily functions as a constituent of heteromeric TRPM6/7 channels. However, heterologous expression of the human TRPM6 protein engendered controversial results with respect to channel characteristics including its regulation by Mg(2+) and Mg·ATP. To resolve this issue, we cloned the mouse TRPM6 (mTRPM6) cDNA and compared its functional characteristics to mouse TRPM7 (mTRPM7) after heterologous expression. Notably, we observed that mTRPM6 and mTRPM7 differentially regulate properties of heteromeric mTRPM6/7 channels: In the presence of mTRPM7, the extreme sensitivity of functionally expressed homomeric mTRPM6 to Mg(2+) is tuned to higher concentrations, whereas mTRPM6 relieves mTRPM7 from the tight inhibition by Mg·ATP. Consequently, the association of mTRPM6 with mTRPM7 allows for high constitutive activity of mTRPM6/7 in the presence of physiological levels of Mg(2+) and Mg·ATP, thus laying the mechanistic foundation for constant vectorial Mg(2+) transport specifically into epithelial cells. |*Protein Multimerization [MESH] |Adenosine Triphosphatases/*metabolism [MESH] |Animals [MESH] |Cell Line [MESH] |Cytosol/metabolism [MESH] |Gene Expression [MESH] |Humans [MESH] |Magnesium/*metabolism [MESH] |Mice [MESH] |Models, Molecular [MESH] |Permeability [MESH] |Protein Conformation [MESH] |Protein Serine-Threonine Kinases/chemistry/metabolism [MESH] |TRPM Cation Channels/chemistry/genetics/*metabolism [MESH]TRPM6 and TRPM7 differentially contribute to the relief of heteromeric(epmc).pdf DeepDyve Pubget Overpricing