Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.ceca.2006.10.003 http://scihub22266oqcxt.onion/10.1016/j.ceca.2006.10.003 17098283!ä!17098283 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       Cell+Calcium 2007 ; 41 (6): 513-23 Nephropedia Template TP {{tp|p=17098283|t=2007. Molecular determinants of permeation through the cation channel TRPM6 |pdf=|usr=}}{{17098283}} gab.com Text Molecular determinants of permeation through the cation channel TRPM6 JO: Cell Calcium http://www.kidney.de/pget.php?&tw=1&pmid=17098283 #FOAvip TRPM6 and its closest relative TRPM7 are members of the Transient Receptor Potential Melastatin (TRPM) subfamily of cation channels and are known to be Mg2+ permeable. By aligning the sequence of the putative TRPM6 pore with the pore sequences of the other subfamily members, we located in the loop between the fifth and the sixth transmembrane domain, a stretch of amino acids residues, 1028GEIDVC1033, as the potential selectivity filter. Two negatively charged residues, E1024 (conserved in TRPM6, TRPM7, TRPM1 and TRPM3) and D1031 (conserved along the entire TRPM subfamily), were identified as important determinants of cation permeation through TRPM6, because neutralization of both residues into an alanine resulted in non-functional channels. Neutralization of E1029 (conserved in TRPM6, TRPM7, TRPM4 and TRPM5) resulted in channels with increased conductance for Ba2+ and Zn2+, decreased ruthenium red sensitivity and larger pore diameter compared to wild-type TRPM6. Changing the residue I1030 into methionine, resulted in channels with lower conductance for Ni2+, decreased sensitivity to ruthenium red block and reduced pore diameter. Thus, these data demonstrate that amino acid residues E1024, I1030 and D1031 are important for channel function and that subtle amino acid variation in the pore region accounts for TRPM6 permeation properties. Twit Text FOAVip Molecular determinants of permeation through the cation channel TRPM6 ????Cell Calcium http://www.kidney.de/pget.php?&tw=1&pmid=17098283 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17098283 #FOAvip English Wikipedia <ref>{{Cite pmid|17098283}}</ref> Molecular determinants of permeation through the cation channel TRPM6 #MMPMID17098283 Topala CN; Groenestege WT; Thebault S; van den Berg D; Nilius B; Hoenderop JG; Bindels RJ Cell Calcium 2007[Jun]; 41 (6): 513-23 PMID17098283show ga TRPM6 and its closest relative TRPM7 are members of the Transient Receptor Potential Melastatin (TRPM) subfamily of cation channels and are known to be Mg2+ permeable. By aligning the sequence of the putative TRPM6 pore with the pore sequences of the other subfamily members, we located in the loop between the fifth and the sixth transmembrane domain, a stretch of amino acids residues, 1028GEIDVC1033, as the potential selectivity filter. Two negatively charged residues, E1024 (conserved in TRPM6, TRPM7, TRPM1 and TRPM3) and D1031 (conserved along the entire TRPM subfamily), were identified as important determinants of cation permeation through TRPM6, because neutralization of both residues into an alanine resulted in non-functional channels. Neutralization of E1029 (conserved in TRPM6, TRPM7, TRPM4 and TRPM5) resulted in channels with increased conductance for Ba2+ and Zn2+, decreased ruthenium red sensitivity and larger pore diameter compared to wild-type TRPM6. Changing the residue I1030 into methionine, resulted in channels with lower conductance for Ni2+, decreased sensitivity to ruthenium red block and reduced pore diameter. Thus, these data demonstrate that amino acid residues E1024, I1030 and D1031 are important for channel function and that subtle amino acid variation in the pore region accounts for TRPM6 permeation properties. |Amino Acid Sequence[MESH] |Cations/metabolism[MESH] |Cell Line[MESH] |Humans[MESH] |Ion Transport[MESH] |Magnesium/*metabolism[MESH] |Molecular Sequence Data[MESH] |Mutation[MESH] |Patch-Clamp Techniques[MESH] |Ruthenium Red/pharmacology[MESH] |Sequence Alignment[MESH] |Sodium/metabolism[MESH] |TRPM Cation Channels/*chemistry/genetics/*metabolism[MESH]Molecular determinants of permeation through the cation channel TRPM6 (epmc).pdf DeepDyve Pubget Overpricing