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10.1093/emboj/16.6.1145 http://scihub22266oqcxt.onion/10.1093/emboj/16.6.1145 9135131!1169713!9135131     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       EMBO+J 1997 ; 16 (6): 1145-52 Nephropedia Template TP {{tp|p=9135131|t=1997. The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide |pdf=|usr=}}{{9135131}} gab.com Text The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=9135131 #FOAvip The ATP-sensitive K-channel (K-ATP channel) plays a key role in insulin secretion from pancreatic beta-cells. It is closed by glucose metabolism, which stimulates insulin secretion, and opened by the drug diazoxide, which inhibits insulin release. Metabolic regulation is mediated by changes in ATP and Mg-ADP, which inhibit and potentiate channel activity, respectively. The beta-cell K-ATP channel consists of a pore-forming subunit, Kir6.2, and a regulatory subunit, SUR1. We have mutated (independently or together) two lysine residues in the Walker A (W(A)) motifs of the first (K719A) and second (K1384M) nucleotide-binding domains (NBDs) of SUR1. These mutations are expected to inhibit nucleotide hydrolysis. Our results indicate that the W(A) lysine of NBD1 (but not NBD2) is essential for activation of K-ATP currents by diazoxide. The potentiatory effects of Mg-ADP required the presence of the W(A) lysines in both NBDs. Mutant currents were slightly more sensitive to ATP than wild-type currents. Metabolic inhibition led to activation of wild-type and K1384M currents, but not K719A or K719A/K1384M currents, suggesting that there may be a factor in addition to ATP and ADP which regulates K-ATP channel activity. Twit Text FOAVip The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=9135131 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=9135131 #FOAvip English Wikipedia <ref>{{Cite pmid|9135131}}</ref> The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide #MMPMID9135131 Gribble FM; Tucker SJ; Ashcroft FM EMBO J 1997[Mar]; 16 (6): 1145-52 PMID9135131show ga The ATP-sensitive K-channel (K-ATP channel) plays a key role in insulin secretion from pancreatic beta-cells. It is closed by glucose metabolism, which stimulates insulin secretion, and opened by the drug diazoxide, which inhibits insulin release. Metabolic regulation is mediated by changes in ATP and Mg-ADP, which inhibit and potentiate channel activity, respectively. The beta-cell K-ATP channel consists of a pore-forming subunit, Kir6.2, and a regulatory subunit, SUR1. We have mutated (independently or together) two lysine residues in the Walker A (W(A)) motifs of the first (K719A) and second (K1384M) nucleotide-binding domains (NBDs) of SUR1. These mutations are expected to inhibit nucleotide hydrolysis. Our results indicate that the W(A) lysine of NBD1 (but not NBD2) is essential for activation of K-ATP currents by diazoxide. The potentiatory effects of Mg-ADP required the presence of the W(A) lysines in both NBDs. Mutant currents were slightly more sensitive to ATP than wild-type currents. Metabolic inhibition led to activation of wild-type and K1384M currents, but not K719A or K719A/K1384M currents, suggesting that there may be a factor in addition to ATP and ADP which regulates K-ATP channel activity. |Adenosine Diphosphate/*pharmacology[MESH] |Adenosine Monophosphate/pharmacology[MESH] |Adenosine Triphosphate/*metabolism/pharmacology[MESH] |Animals[MESH] |Antimetabolites/pharmacology[MESH] |Azides/pharmacology[MESH] |Cloning, Molecular[MESH] |Diazoxide/*pharmacology[MESH] |Female[MESH] |In Vitro Techniques[MESH] |Insulin Secretion[MESH] |Insulin/metabolism[MESH] |Islets of Langerhans/metabolism[MESH] |Kinetics[MESH] |Magnesium/pharmacology[MESH] |Mice[MESH] |Mutagenesis, Site-Directed[MESH] |Oocytes/metabolism[MESH] |Potassium Channels/*chemistry/genetics/*metabolism[MESH] |Protein Conformation[MESH] |Rats[MESH] |Sodium Azide[MESH]The essential role of the Walker A motifs of SUR1 in K-ATP channel act(epmc).pdf DeepDyve Pubget Overpricing