Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.

Summary Expression Phenotypes Gene Literature (112) GO Terms (6) Nucleotides (46) Proteins (32) Interactants (165) Wiki
XB--6084576

Papers associated with kcnj11



???displayGene.coCitedPapers???

???pagination.result.count???

???pagination.result.page??? ???pagination.result.prev??? 1 2 3

Sort Newest To Oldest Sort Oldest To Newest

The novel diazoxide analog 3-isopropylamino-7-methoxy-4H-1,2,4-benzothiadiazine 1,1-dioxide is a selective Kir6.2/SUR1 channel opener., Dabrowski M, Ashcroft FM, Ashfield R, Lebrun P, Pirotte B, Egebjerg J, Bondo Hansen J, Wahl P., Diabetes. June 1, 2002; 51 (6): 1896-906.

Allosteric modulation of the mouse Kir6.2 channel by intracellular H+ and ATP., Wu J, Cui N, Piao H, Wang Y, Xu H, Mao J, Jiang C., J Physiol. September 1, 2002; 543 (Pt 2): 495-504.

Protons activate homomeric Kir6.2 channels by selective suppression of the long and intermediate closures., Wu J, Xu H, Yang Z, Wang Y, Mao J, Jiang C., J Membr Biol. November 15, 2002; 190 (2): 105-16.

K(ATP) channel activity is required for hatching in Xenopus embryos., Cheng SM, Chen I, Levin M., Dev Dyn. December 1, 2002; 225 (4): 588-91.        

A threonine residue (Thr71) at the intracellular end of the M1 helix plays a critical role in the gating of Kir6.2 channels by intracellular ATP and protons., Cui N, Wu J, Xu H, Wang R, Rojas A, Piao H, Mao J, Abdulkadir L, Li L, Jiang C., J Membr Biol. March 15, 2003; 192 (2): 111-22.

Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels., Konstas AA, Korbmacher C, Tucker SJ., Am J Physiol Cell Physiol. April 1, 2003; 284 (4): C910-7.

Identification of residues contributing to the ATP binding site of Kir6.2., Trapp S, Haider S, Jones P, Sansom MS, Ashcroft FM., EMBO J. June 16, 2003; 22 (12): 2903-12.

Pyridine nucleotide regulation of the KATP channel Kir6.2/SUR1 expressed in Xenopus oocytes., Dabrowski M, Trapp S, Ashcroft FM., J Physiol. July 15, 2003; 550 (Pt 2): 357-63.

Na(+) current through KATP channels: consequences for Na(+) and K(+) fluxes during early myocardial ischemia., Bollensdorff C, Knopp A, Biskup C, Zimmer T, Benndorf K., Am J Physiol Heart Circ Physiol. January 1, 2004; 286 (1): H283-95.

Concerted gating mechanism underlying KATP channel inhibition by ATP., Drain P, Geng X, Li L., Biophys J. April 1, 2004; 86 (4): 2101-12.

Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes., Gloyn AL, Pearson ER, Antcliff JF, Proks P, Bruining GJ, Slingerland AS, Howard N, Srinivasan S, Silva JM, Molnes J, Edghill EL, Frayling TM, Temple IK, Mackay D, Shield JP, Sumnik Z, van Rhijn A, Wales JK, Clark P, Gorman S, Aisenberg J, Ellard S, Njølstad PR, Ashcroft FM, Hattersley AT., N Engl J Med. April 29, 2004; 350 (18): 1838-49.

Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2., Dabrowski M, Tarasov A, Ashcroft FM., J Physiol. June 1, 2004; 557 (Pt 2): 347-54.

Arylcyanoguanidines as activators of Kir6.2/SUR1K ATP channels and inhibitors of insulin release., Tagmose TM, Schou SC, Mogensen JP, Nielsen FE, Arkhammar PO, Wahl P, Hansen BS, Worsaae A, Boonen HC, Antoine MH, Lebrun P, Hansen JB., J Med Chem. June 3, 2004; 47 (12): 3202-11.

Molecular basis of inward rectification: polyamine interaction sites located by combined channel and ligand mutagenesis., Kurata HT, Phillips LR, Rose T, Loussouarn G, Herlitze S, Fritzenschaft H, Enkvetchakul D, Nichols CG, Baukrowitz T., J Gen Physiol. November 1, 2004; 124 (5): 541-54.                

Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features., Proks P, Antcliff JF, Lippiat J, Gloyn AL, Hattersley AT, Ashcroft FM., Proc Natl Acad Sci U S A. December 14, 2004; 101 (50): 17539-44.

Determinant role of membrane helices in K ATP channel gating., Wang R, Rojas A, Wu J, Piao H, Adams CY, Xu H, Shi Y, Shi Y, Wang Y, Jiang C., J Membr Biol. March 1, 2005; 204 (1): 1-10.

Relapsing diabetes can result from moderately activating mutations in KCNJ11., Gloyn AL, Reimann F, Girard C, Edghill EL, Proks P, Pearson ER, Temple IK, Mackay DJ, Shield JP, Freedenberg D, Noyes K, Ellard S, Ashcroft FM, Gribble FM, Hattersley AT., Hum Mol Genet. April 1, 2005; 14 (7): 925-34.

A gating mutation at the internal mouth of the Kir6.2 pore is associated with DEND syndrome., Proks P, Girard C, Haider S, Gloyn AL, Hattersley AT, Sansom MS, Ashcroft FM., EMBO Rep. May 1, 2005; 6 (5): 470-5.

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions., Tammaro P, Girard C, Molnes J, Njølstad PR, Ashcroft FM., EMBO J. July 6, 2005; 24 (13): 2318-30.

Ligand-dependent linkage of the ATP site to inhibition gate closure in the KATP channel., Li L, Geng X, Yonkunas M, Su A, Densmore E, Tang P, Drain P., J Gen Physiol. September 1, 2005; 126 (3): 285-99.                  

Functional effects of KCNJ11 mutations causing neonatal diabetes: enhanced activation by MgATP., Proks P, Girard C, Ashcroft FM., Hum Mol Genet. September 15, 2005; 14 (18): 2717-26.

Kir6.2 channel gating by intracellular protons: subunit stoichiometry for ligand binding and channel gating., Wang R, Su J, Zhang X, Shi Y, Cui N, Onyebuchi VA, Jiang C., J Membr Biol. January 1, 2006; 213 (3): 155-64.

Functional effects of naturally occurring KCNJ11 mutations causing neonatal diabetes on cloned cardiac KATP channels., Tammaro P, Proks P, Ashcroft FM., J Physiol. February 15, 2006; 571 (Pt 1): 3-14.

Functional effects of mutations at F35 in the NH2-terminus of Kir6.2 (KCNJ11), causing neonatal diabetes, and response to sulfonylurea therapy., Proks P, Girard C, Baevre H, Njølstad PR, Ashcroft FM., Diabetes. June 1, 2006; 55 (6): 1731-7.

Mutations at the same residue (R50) of Kir6.2 (KCNJ11) that cause neonatal diabetes produce different functional effects., Shimomura K, Girard CA, Proks P, Nazim J, Lippiat JD, Cerutti F, Lorini R, Ellard S, Hattersley AT, Barbetti F, Ashcroft FM., Diabetes. June 1, 2006; 55 (6): 1705-12.

A heterozygous activating mutation in the sulphonylurea receptor SUR1 (ABCC8) causes neonatal diabetes., Proks P, Arnold AL, Bruining J, Girard C, Flanagan SE, Larkin B, Colclough K, Hattersley AT, Ashcroft FM, Ellard S., Hum Mol Genet. June 1, 2006; 15 (11): 1793-800.

Switching from insulin to oral sulfonylureas in patients with diabetes due to Kir6.2 mutations., Pearson ER, Flechtner I, Njølstad PR, Malecki MT, Flanagan SE, Larkin B, Ashcroft FM, Klimes I, Codner E, Iotova V, Slingerland AS, Shield J, Robert JJ, Holst JJ, Clark PM, Ellard S, Søvik O, Polak M, Hattersley AT, Neonatal Diabetes International Collaborative Group., N Engl J Med. August 3, 2006; 355 (5): 467-77.

Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels., Heusser K, Yuan H, Neagoe I, Tarasov AI, Ashcroft FM, Schwappach B., J Cell Sci. October 15, 2006; 119 (Pt 20): 4353-63.

The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels., Fang K, Csanády L, Chan KW., J Physiol. October 15, 2006; 576 (Pt 2): 379-89.

Functional analysis of six Kir6.2 (KCNJ11) mutations causing neonatal diabetes., Girard CA, Shimomura K, Proks P, Absalom N, Castano L, Perez de Nanclares G, Ashcroft FM., Pflugers Arch. December 1, 2006; 453 (3): 323-32.

Subunit-stoichiometric evidence for kir6.2 channel gating, ATP binding, and binding-gating coupling., Wang R, Zhang X, Cui N, Wu J, Piao H, Wang X, Su J, Jiang C., Mol Pharmacol. June 1, 2007; 71 (6): 1646-56.

The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits., Tammaro P, Ashcroft F., J Physiol. June 15, 2007; 581 (Pt 3): 1259-69.

Remodelling of the SUR-Kir6.2 interface of the KATP channel upon ATP binding revealed by the conformational blocker rhodamine 123., Hosy E, Dérand R, Revilloud J, Vivaudou M., J Physiol. July 1, 2007; 582 (Pt 1): 27-39.

Iptakalim, a vascular ATP-sensitive potassium (KATP) channel opener, closes rat pancreatic beta-cell KATP channels and increases insulin release., Misaki N, Mao X, Lin YF, Suga S, Li GH, Liu Q, Chang Y, Wang H, Wakui M, Wu J., J Pharmacol Exp Ther. August 1, 2007; 322 (2): 871-8.

Single residue (K332A) substitution in Kir6.2 abolishes the stimulatory effect of long-chain acyl-CoA esters: indications for a long-chain acyl-CoA ester binding motif., Bränström R, Leibiger IB, Leibiger B, Klement G, Nilsson J, Arhem P, Aspinwall CA, Corkey BE, Larsson O, Berggren PO., Diabetologia. August 1, 2007; 50 (8): 1670-7.

A novel mutation causing DEND syndrome: a treatable channelopathy of pancreas and brain., Shimomura K, Hörster F, de Wet H, Flanagan SE, Ellard S, Hattersley AT, Wolf NI, Ashcroft F, Ebinger F., Neurology. September 25, 2007; 69 (13): 1342-9.

Functional analysis of two Kir6.2 (KCNJ11) mutations, K170T and E322K, causing neonatal diabetes., Tarasov AI, Girard CA, Larkin B, Tammaro P, Flanagan SE, Ellard S, Ashcroft FM., Diabetes Obes Metab. November 1, 2007; 9 Suppl 2 46-55.

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit., Tammaro P, Ashcroft FM., J Physiol. November 1, 2007; 584 (Pt 3): 743-53.

Sulfonylurea receptors type 1 and 2A randomly assemble to form heteromeric KATP channels of mixed subunit composition., Chan KW, Wheeler A, Csanády L., J Gen Physiol. January 1, 2008; 131 (1): 43-58.                    

A Kir6.2 mutation causing severe functional effects in vitro produces neonatal diabetes without the expected neurological complications., Tammaro P, Flanagan SE, Zadek B, Srinivasan S, Woodhead H, Hameed S, Klimes I, Hattersley AT, Ellard S, Ashcroft FM., Diabetologia. May 1, 2008; 51 (5): 802-10.            

Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2., Dupuis JP, Revilloud J, Moreau CJ, Vivaudou M., J Physiol. July 1, 2008; 586 (13): 3075-85.

How ATP inhibits the open K(ATP) channel., Craig TJ, Ashcroft FM, Proks P., J Gen Physiol. July 1, 2008; 132 (1): 131-44.            

Effects of sodium azide, barium ion, d-amphetamine and procaine on inward rectifying potassium channel 6.2 expressed in Xenopus oocytes., Kung FL, Tsai JL, Lee CH, Lee CH, Lou KL, Tang CY, Liou HH, Lu KL, Chen YH, Wang WJ, Tsai MC., J Formos Med Assoc. August 1, 2008; 107 (8): 600-8.

A cytosolic factor that inhibits KATP channels expressed in Xenopus oocytes by impairing Mg-nucleotide activation by SUR1., Tammaro P, Ashcroft FM., J Physiol. April 15, 2009; 587 (Pt 8): 1649-56.

An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1., Craig TJ, Shimomura K, Holl RW, Flanagan SE, Ellard S, Ashcroft FM., J Clin Endocrinol Metab. July 1, 2009; 94 (7): 2551-7.

The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP-binding residue., Shimomura K, de Nanclares GP, Foutinou C, Caimari M, Castaño L, Ashcroft FM., Diabet Med. February 1, 2010; 27 (2): 225-9.

Targeting hypertension with a new adenosine triphosphate-sensitive potassium channel opener iptakalim., Pan Z, Huang J, Cui W, Long C, Zhang Y, Wang H., J Cardiovasc Pharmacol. September 1, 2010; 56 (3): 215-28.

Disease progression and search for monogenic diabetes among children with new onset type 1 diabetes negative for ICA, GAD- and IA-2 Antibodies., Pörksen S, Laborie LB, Nielsen L, Louise Max Andersen M, Sandal T, de Wet H, Schwarcz E, Aman J, Swift P, Kocova M, Schönle EJ, de Beaufort C, Hougaard P, Ashcroft F, Molven A, Knip M, Mortensen HB, Hansen L, Njølstad PR, Hvidøre Study Group on Childhood Diabetes., BMC Endocr Disord. September 23, 2010; 10 16.      

Activation of the K(ATP) channel by Mg-nucleotide interaction with SUR1., Proks P, de Wet H, Ashcroft FM., J Gen Physiol. October 1, 2010; 136 (4): 389-405.                    

β2-Adrenergic ion-channel coupled receptors as conformational motion detectors., Caro LN, Moreau CJ, Revilloud J, Vivaudou M., PLoS One. March 9, 2011; 6 (3): e18226.            

???pagination.result.page??? ???pagination.result.prev??? 1 2 3