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10.1093/emboj/cdg376 http://scihub22266oqcxt.onion/10.1093/emboj/cdg376 12881418!169049!12881418     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2003 ; 22 (15): 3833-43 Nephropedia Template TP {{tp|p=12881418|t=2003. N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits |pdf=|usr=}}{{12881418}} gab.com Text N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=12881418 #FOAvip The sulfonylurea receptor (SUR), an ATP-binding cassette (ABC) protein, assembles with a potassium channel subunit (Kir6) to form the ATP-sensitive potassium channel (K(ATP)) complex. Although SUR is an important regulator of Kir6, the specific SUR domain that associates with Kir6 is still unknown. All functional ABC proteins contain two transmembrane domains but some, including SUR and MRP1 (multidrug resistance protein 1), contain an extra N-terminal transmembrane domain called TMD0. The functions of any TMD0s are largely unclear. Using Xenopus oocytes to coexpress truncated SUR constructs with Kir6, we demonstrated by immunoprecipitation, single-oocyte chemiluminescence and electrophysiological measurements that the TMD0 of SUR1 strongly associated with Kir6.2 and modulated its trafficking and gating. Two TMD0 mutations, A116P and V187D, previously correlated with persistent hyperinsulinemic hypoglycemia of infancy, were found to disrupt the association between TMD0 and Kir6.2. These results underscore the importance of TMD0 in K(ATP) channel function, explaining how specific mutations within this domain result in disease, and suggest how an ABC protein has evolved to regulate a potassium channel. Twit Text FOAVip N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=12881418 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=12881418 #FOAvip English Wikipedia <ref>{{Cite pmid|12881418}}</ref> N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits #MMPMID12881418 Chan KW; Zhang H; Logothetis DE EMBO J 2003[Aug]; 22 (15): 3833-43 PMID12881418show ga The sulfonylurea receptor (SUR), an ATP-binding cassette (ABC) protein, assembles with a potassium channel subunit (Kir6) to form the ATP-sensitive potassium channel (K(ATP)) complex. Although SUR is an important regulator of Kir6, the specific SUR domain that associates with Kir6 is still unknown. All functional ABC proteins contain two transmembrane domains but some, including SUR and MRP1 (multidrug resistance protein 1), contain an extra N-terminal transmembrane domain called TMD0. The functions of any TMD0s are largely unclear. Using Xenopus oocytes to coexpress truncated SUR constructs with Kir6, we demonstrated by immunoprecipitation, single-oocyte chemiluminescence and electrophysiological measurements that the TMD0 of SUR1 strongly associated with Kir6.2 and modulated its trafficking and gating. Two TMD0 mutations, A116P and V187D, previously correlated with persistent hyperinsulinemic hypoglycemia of infancy, were found to disrupt the association between TMD0 and Kir6.2. These results underscore the importance of TMD0 in K(ATP) channel function, explaining how specific mutations within this domain result in disease, and suggest how an ABC protein has evolved to regulate a potassium channel. |*ATP-Binding Cassette Transporters[MESH] |*Ion Channel Gating[MESH] |Adenosine Diphosphate/pharmacology[MESH] |Adenosine Triphosphate/pharmacology[MESH] |Animals[MESH] |Diazoxide/pharmacology[MESH] |Glyburide/*pharmacology[MESH] |Mutagenesis, Site-Directed[MESH] |Potassium Channels, Inwardly Rectifying/drug effects/genetics/*physiology[MESH] |Potassium Channels/chemistry/genetics/*physiology[MESH] |Receptors, Drug/chemistry/genetics/*physiology[MESH] |Sulfonylurea Receptors[MESH]N-terminal transmembrane domain of the SUR controls trafficking and ga(epmc).pdf DeepDyve Pubget Overpricing