Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
about
The Nucleotide-Binding Sites of SUR1: A Mechanistic ModelMapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactionsProximal C-terminal domain of sulphonylurea receptor 2A interacts with pore-forming Kir6 subunits in KATP channelsEngineered Kir6.2 mutations that correct the trafficking defect of K(ATP) channels caused by specific SUR1 mutationsRat homolog of sulfonylurea receptor 2B determines glibenclamide sensitivity of ROMK2 in Xenopus laevis oocyte.Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay.Mutations in the linker domain of NBD2 of SUR inhibit transduction but not nucleotide bindingThe I182 region of k(ir)6.2 is closely associated with ligand binding in K(ATP) channel inhibition by ATPConcerted gating mechanism underlying KATP channel inhibition by ATP.The molecular mechanisms and pharmacotherapy of ATP-sensitive potassium channel gene mutations underlying neonatal diabetesMuscle KATP channels: recent insights to energy sensing and myoprotectionStructurally distinct ligands rescue biogenesis defects of the KATP channel complex via a converging mechanism.Mechanism of KATP hyperactivity and sulfonylurea tolerance due to a diabetogenic mutation in L0 helix of sulfonylurea receptor 1 (ABCC8)The role of NH2-terminal positive charges in the activity of inward rectifier KATP channelsRegulation of cloned ATP-sensitive K channels by adenine nucleotides and sulfonylureas: interactions between SUR1 and positively charged domains on Kir6.2.Ligand-dependent linkage of the ATP site to inhibition gate closure in the KATP channelA Kir6.2 mutation causing severe functional effects in vitro produces neonatal diabetes without the expected neurological complicationsReview. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.Pharmacological rescue of trafficking-impaired ATP-sensitive potassium channels.An amino acid triplet in the NH2 terminus of rat ROMK1 determines interaction with SUR2B.The shifting landscape of KATP channelopathies and the need for 'sharper' therapeutics.Secondary consequences of beta cell inexcitability: identification and prevention in a murine model of K(ATP)-induced neonatal diabetes mellitus.A shaker-like K(+) channel with weak rectification is expressed in both source and sink phloem tissues of Arabidopsis.Rebuilding a macromolecular membrane complex at the atomic scale: case of the Kir6.2 potassium channel coupled to the muscarinic acetylcholine receptor M2.Incomplete dissociation of glibenclamide from wild-type and mutant pancreatic K ATP channels limits their recovery from inhibition.Analysis of two KCNJ11 neonatal diabetes mutations, V59G and V59A, and the analogous KCNJ8 I60G substitution: differences between the channel subtypes formed with SUR1.Sulfonylureas correct trafficking defects of disease-causing ATP-sensitive potassium channels by binding to the channel complex.ATP-sensitive K+ channels: regulation of bursting by the sulphonylurea receptor, PIP2 and regions of Kir6.2.ATP sensitivity of ATP-sensitive K+ channels: role of the gamma phosphate group of ATP and the R50 residue of mouse Kir6.2.A region of the sulfonylurea receptor critical for a modulation of ATP-sensitive K(+) channels by G-protein betagamma-subunits.Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels.The mutation Y1206S increases the affinity of the sulphonylurea receptor SUR2A for glibenclamide and enhances the effects of coexpression with Kir6.2.Molecular mechanism of sulphonylurea block of K(ATP) channels carrying mutations that impair ATP inhibition and cause neonatal diabetes.The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits.Anti-diabetic drug binding site in a mammalian KATP channel revealed by Cryo-EM.Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.Mechanism of Kir6.2 channel inhibition by sulfhydryl modification: pore block or allosteric gating?Analysis of the differential modulation of sulphonylurea block of beta-cell and cardiac ATP-sensitive K+ (K(ATP)) channels by Mg-nucleotides.Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
P2860
Q26774807-DF6117A0-03DC-487E-991B-3774A7DE571BQ28137825-500B64DF-FD47-441D-83DB-3C04A08EBB6EQ28565185-467DBCC9-7421-4FED-A903-A6014687C737Q28572793-8BA99152-A026-47CD-97F1-46C0A11DF1BBQ28941209-1F27FD12-DF3E-401D-944E-128FD64B462DQ30854923-2216ECC8-01FE-4715-8234-1915CE45418AQ33661454-B28A54A3-CE96-46C0-8616-5750FE5B0474Q34079244-918D3ED7-A26B-4A7F-B687-43D661AC637DQ34173659-258B9B22-8B71-471C-AC07-23882B4D82BEQ34185246-FB122000-0EF7-49FA-91B6-69C8C1E10CA7Q34316689-1E8F94C9-2F02-45B6-869B-36AA7103170CQ35076166-61B85DAF-4CD0-40A8-9B15-63FF7761F894Q35199497-C7F89C34-0EC0-4BE1-9FAB-8E6DBFF6E3E3Q35549132-3CFA589C-FA78-4780-8DFB-31B3CA483613Q36436454-9F2902B1-9C85-433C-B512-707E4D11B6E9Q36444788-BB91B090-E7D7-4D11-90A6-99012E2CB9C0Q36493543-2B66BBC4-5A05-434D-8592-3DD03413C134Q36538371-567CC95D-589C-4564-A418-EAAE9BCB4487Q37319861-432136DE-8398-4DFA-AED2-FC85E0829537Q37409971-9B44F2C3-98E9-46E5-93ED-786EAE69B8E3Q38296629-1330884A-E381-4FFA-A1AE-2F48DEA724B0Q38869442-DEE1BF58-FC70-4E35-BE6C-69D7781F6535Q39035715-D2CCAA31-796B-4806-AD6A-0B7063E56AB3Q39156012-4CB77F13-5285-4A00-8A09-88D1A2F327B5Q39263823-EDCB0183-1854-4F15-8F28-03C34B276B12Q39893357-A274470E-10C3-4CCF-AAFF-FF133FE4CE9AQ39896293-CD5314E1-4FBA-44AD-A3DF-F0F66A43C82CQ40234875-9F1CD94F-935F-4DC6-B204-8ADE85756B7DQ40337022-94F6D9C0-06B7-402F-80F1-FE4763913794Q40372990-474B292E-E37A-45DD-A7E6-06BF2FA84E12Q40431395-96986368-857C-4564-981B-488B957353DAQ40464415-371E3F2A-307B-4044-953A-C0F71C738B66Q41828259-A5F89FE4-537D-4C56-A383-74A65A247EA9Q42126795-00FBF11D-3C49-4FF9-9193-5ADA55E79A76Q42616038-3F4F0FBB-341F-48E1-A095-42BD16F0F6AEQ42637813-6EE45F1C-5188-4BA5-ADEA-4F92C67BAF9DQ43854347-20E228C2-0EB7-457E-BAEC-5647700003F8Q43977779-0C2758A9-A03E-4126-9AB2-67B405A44AA4Q44300236-4C8061EE-9E0E-4A7C-BB4C-72AF713EDE56Q44788689-CF32DACC-7E99-4CE4-882F-B55D41B15EEF
P2860
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@en
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@nl
type
label
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@en
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@nl
prefLabel
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@en
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@nl
P2860
P1476
Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
@en
P2093
P2860
P304
P356
10.1111/J.1469-7793.1999.0325P.X
P407
P478
518 ( Pt 2)
P577
1999-07-01T00:00:00Z