Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
about
How highly charged anionic lipids bind and regulate ion channelsRunning out of time: the decline of channel activity and nucleotide activation in adenosine triphosphate-sensitive K-channelsThe carboxyl termini of K(ATP) channels bind nucleotidesNovel nucleotide-binding sites in ATP-sensitive potassium channels formed at gating interfaces.Molecular diversity and regulation of renal potassium channels.Concerted gating mechanism underlying KATP channel inhibition by ATP.Seizure-induced reduction in PIP3 levels contributes to seizure-activity and is rescued by valproic acid.Dual-mode phospholipid regulation of human inward rectifying potassium channelsEnhanced PIP3 signaling in POMC neurons causes KATP channel activation and leads to diet-sensitive obesity.Central insulin action in energy and glucose homeostasis.A Kir6.2 pore mutation causes inactivation of ATP-sensitive potassium channels by disrupting PIP2-dependent gating.Muscle KATP channels: recent insights to energy sensing and myoprotectionUnidirectional photoreceptor-to-Müller glia coupling and unique K+ channel expression in Caiman retina.Calcium-dependent inhibition of adrenal TREK-1 channels by angiotensin II and ionomycin.Gating mechanism of KATP channels: function fits form.Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels.KATP Channels in the Cardiovascular System.Stabilization of the activity of ATP-sensitive potassium channels by ion pairs formed between adjacent Kir6.2 subunits.Hydrolyzable ATP and PIP(2) modulate the small-conductance K+ channel in apical membranes of rat cortical-collecting duct (CCD).Regulation of the epithelial Na+ channel (ENaC) by phosphatidylinositides.Ligand-dependent linkage of the ATP site to inhibition gate closure in the KATP channelSupervised membrane swimming: small G-protein lifeguards regulate PIPK signalling and monitor intracellular PtdIns(4,5)P2 pools.Binding and direct activation of the epithelial Na+ channel (ENaC) by phosphatidylinositides.DEND mutation in Kir6.2 (KCNJ11) reveals a flexible N-terminal region critical for ATP-sensing of the KATP channel.Complex roles of PIP2 in the regulation of ion channels and transporters.Neurocircuits integrating hormone and nutrient signaling in control of glucose metabolism.Phosphoinositide regulation of non-canonical transient receptor potential channels.A comprehensive guide to the ROMK potassium channel: form and function in health and disease.CNS regulation of glucose homeostasis.Polyamine effects on cell function: Possible central role of plasma membrane PI(4,5)P2.Channelopathies linked to plasma membrane phosphoinositides.Sensing the fuels: glucose and lipid signaling in the CNS controlling energy homeostasisAnalysis of two KCNJ11 neonatal diabetes mutations, V59G and V59A, and the analogous KCNJ8 I60G substitution: differences between the channel subtypes formed with SUR1.Glucose and insulin synergistically activate phosphatidylinositol 3-kinase to trigger oscillations of phosphatidylinositol 3,4,5-trisphosphate in beta-cells.ATP-sensitive K+ channels: regulation of bursting by the sulphonylurea receptor, PIP2 and regions of Kir6.2.Molecular determinants of cardiac K(ATP) channel activation by epoxyeicosatrienoic acids.Allosteric modulation of the mouse Kir6.2 channel by intracellular H+ and ATP.Antagonistic regulation of native Ca2+- and ATP-sensitive cation channels in brain capillaries by nucleotides and decavanadate.Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening.
P2860
Q24656180-753BCC57-9AFE-4B58-BFA1-31D214C832B5Q26744692-1B16E8CA-80B4-494D-9F4D-55FED4538719Q28214861-72314C33-FD07-4E6C-BAE1-2339C48910E7Q28564824-8C6B3DC9-0982-4E02-AB34-9F259F0D9DB5Q33728388-90A201BF-39F6-495B-B424-D0B208814476Q34185246-AAC4BE7D-763C-4FB7-8A65-4EDD0E9E6A67Q34379505-6955BB47-F68B-4AC5-B956-313A7F3A8D37Q34535871-C8C41A3C-7578-430A-85D6-B5D82161E47AQ34691534-43167BC8-89EE-4F29-8D16-707F04E740FCQ34698802-99DD2B2B-E00F-4857-A7BA-541678202EF4Q34735191-1125CE85-0E1B-4F81-ADCF-6108BBD68CEBQ35076166-C120193D-5C87-42CE-AD31-33C3A2F4C696Q35169151-DEE8DFBF-B0C0-494D-AAFF-D2056871043AQ35216833-EC134B82-3F1A-457E-8F5C-01C550EE4FA6Q35569293-25FB2D7F-8353-44C2-9BBE-62202DD3AD1FQ35799988-8AD7F881-BC03-4DED-BD7F-2E2343B64E1EQ36422478-2A71F37E-001F-4DAA-9ED6-063BDBBBAAB4Q36436497-85FD3290-0FC5-442B-B6C2-27B0A6E2ED16Q36436542-D229A54E-3D86-4980-AACA-A40B9D0AB0E0Q36443034-C2D7EC84-DBE0-435D-9701-0950CC171A42Q36493543-8407166C-C3A3-4E64-B8E5-4B4E67F26ACBQ36542078-2DB0288D-067A-40FA-BDB2-C42C40B98496Q36725869-27DEDA5D-7AE1-43A1-95F5-F9A4C36783B5Q36957386-02406F4D-6ACA-4D9B-88F7-C47D4F66363EQ36967590-1539E89C-9D7A-47A4-B4BF-79F62E971D10Q37088780-0907F475-786F-41BF-9E94-566AD51F9B42Q37289145-9539F2D0-0829-40BD-AF39-10020FA865F6Q37417264-63CE21C5-9FD9-4E6B-B2BA-15B92FC2CDC9Q37512891-AAE34654-7D55-4A9E-8A4F-7148FF07E5F7Q37595417-87FA7868-3856-4169-9D66-C24A47AAD41DQ37732004-9BC7A8CB-E426-4282-86E4-92F93D086663Q37765224-FAC14ADD-1DCA-4177-B5A8-DDEE6566E24DQ39896293-D7D4DCCC-78BA-4F6F-B4D3-37594EB5B704Q40214110-5E3A7A71-BEE7-4EE3-BE9D-DD1B0F87C5CDQ40337022-EA3E9632-EE9E-4A9F-967E-533A310733F2Q40448045-E5B322C0-8285-4F42-A09E-2C910771E031Q40707353-3AB8EE17-59FB-4827-A8BA-D4C949898951Q41954014-A381B83B-C5E6-4546-B54E-DCBAF97B269BQ42411930-04D68B65-6E9D-4299-B69C-0E152AFF3B4AQ42637385-B7872998-AF48-4864-8FDA-20B2BFB85FC4
P2860
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@ast
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@en
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@nl
type
label
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@ast
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@en
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@nl
prefLabel
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@ast
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@en
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@nl
P2093
P2860
P356
P1476
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels.
@en
P2093
Carlos G Vanoye
Gerhard Giebisch
Gordon G MacGregor
LieQi Tang
Steven C Hebert
P2860
P304
P356
10.1073/PNAS.042688899
P407
P577
2002-03-01T00:00:00Z