ATPase activity of the cystic fibrosis transmembrane conductance regulator
about
Cystic Fibrosis: Lessons from the Sweat GlandSelective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770CFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).New and emerging targeted therapies for cystic fibrosisThe yeast a-factor transporter Ste6p, a member of the ABC superfamily, couples ATP hydrolysis to pheromone export.The proposed channel-enzyme transient receptor potential melastatin 2 does not possess ADP ribose hydrolase activityATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)Genome-wide identification, characterization and phylogenetic analysis of 50 catfish ATP-binding cassette (ABC) transporter genesBiochemical characterization of MsbA from Pseudomonas aeruginosaCurcumin and genistein: the combined effects on disease-associated CFTR mutants and their clinical implicationsPerturbation of the pore of the cystic fibrosis transmembrane conductance regulator (CFTR) inhibits its atpase activity.CFTR channel gating: incremental progress in irreversible steps.Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.When an ATPase is not an ATPase: at low temperatures the C-terminal domain of the ABC transporter CvaB is a GTPaseCystic fibrosis transmembrane conductance regulator. Structure and function of an epithelial chloride channel.ADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.Cystic fibrosis transmembrane conductance regulator (CFTR) potentiator VX-770 (ivacaftor) opens the defective channel gate of mutant CFTR in a phosphorylation-dependent but ATP-independent manner.Mutations in the linker domain of NBD2 of SUR inhibit transduction but not nucleotide bindingCysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels.A survey of detergents for the purification of stable, active human cystic fibrosis transmembrane conductance regulator (CFTR).A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.A conditional probability analysis of cystic fibrosis transmembrane conductance regulator gating indicates that ATP has multiple effects during the gating cycle.Correction of G551D-CFTR transport defect in epithelial monolayers by genistein but not by CPX or MPB-07.PharmGKB summary: very important pharmacogene information for CFTRRNA Interference Screen to Identify Kinases That Suppress Rescue of ΔF508-CFTR.ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione.Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle.G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defectsActions of genistein on cystic fibrosis transmembrane conductance regulator channel gating. Evidence for two binding sites with opposite effects.Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel.Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating schemeOn the mechanism of MgATP-dependent gating of CFTR Cl- channelsReversible silencing of CFTR chloride channels by glutathionylation.Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domainsDistinct Mg(2+)-dependent steps rate limit opening and closing of a single CFTR Cl(-) channel.Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Long-range coupling between the extracellular gates and the intracellular ATP binding domains of multidrug resistance protein pumps and cystic fibrosis transmembrane conductance regulator channels
P2860
Q22306467-574A6CDC-F53B-4998-8544-ED877A1F4B4EQ24301098-9710F174-C6C6-4081-9027-D4882A1E46B5Q24644303-15EB186A-BFA2-4AEE-8D35-C27328E6E553Q25256649-219941EF-DF52-4D15-A6CC-0977D9153BB6Q26749278-803C3363-383A-424B-A6E6-9DB894EFAE80Q27936552-21EACD04-3060-470F-812E-9FC9F3850C95Q28116139-F51562DD-03AE-4BFB-B463-9E7B403BEB8CQ28217842-DE6E5B27-1F85-45AC-A0F4-9B3516AA0DF4Q28488138-1BB0105D-B6C5-438F-9AC9-611BF8DF06A0Q28492568-A601F42B-74A3-42B0-89A3-0C5AD237C629Q28830793-59B43C0E-D07F-47FC-A021-47E78F3DB47BQ31743298-33B8D485-388D-46EE-9193-77BF18FBBA99Q33683078-0467B7E5-8DB1-4A69-813D-DEEEF250A4E1Q33723395-3023DB4A-BFF4-4872-937F-69B01E27BA29Q33726448-278B135F-F69C-438A-8587-4E283A1095CDQ33830343-29B828D0-BD01-4808-8EC4-9A233FC9A522Q33838222-CBE0331B-0ABF-47F9-9B71-54D480C174DDQ33931117-A20CD27E-D4AA-4EDA-AE99-0CBC8A57D487Q34033437-1321B303-77BB-40E2-9398-32DE818A0140Q34079244-2B5BD77D-4E9A-49E8-92B1-49A570842292Q34177343-3CE469B2-9584-456D-B31F-95F01814C6A0Q34221261-2B51A163-D4B1-4E91-95F7-ABCD70F2A463Q34262494-FEA0EA48-8EA7-4AE6-ADB6-F698B5FAF5A0Q34755466-4F638388-A694-49BC-8AD6-30C0C443C18AQ35044633-27CE08C3-3975-431F-BA08-331AB2DF4F10Q35108743-CEF31CCE-2355-4684-80AE-7579575C7B35Q35590787-7C53FA3A-1F34-41DE-B2E0-7C03AB18D13AQ35656224-22A204D6-1A7A-44F1-AD44-48340433CFF2Q36295891-F7D10A48-FC9C-4413-983A-8C3FAA30F34BQ36296010-1EA17130-0EBA-4D9C-8EF6-64CB7292E2A0Q36411954-0A904DF2-00AD-4B46-8AF0-695A7B324C3DQ36411989-7D412648-EAE6-49B7-B16B-569BC5C47357Q36412100-648B0879-3957-4EAF-BD79-6CD8E5E8CAF5Q36412358-BF48A0FE-E5E3-41AA-BD5E-84F3620E4148Q36412614-AEC00140-FCB7-41C6-B12C-66BFA9A68FDCQ36444749-422E5D60-500B-4F41-9E0F-58ED735DC1CEQ36445281-464C0314-580D-4880-A9C2-83AC2BF6F9AEQ36447213-71A521A1-D825-4803-8F37-7FBCBFD96348Q36525551-2746A210-FFD0-4E31-826D-0A56F0B83D5CQ36570921-2D1ADAC4-E6DC-46CB-A601-EB419A88D23A
P2860
ATPase activity of the cystic fibrosis transmembrane conductance regulator
description
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1996
@ast
im November 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 1996/11/08)
@nl
наукова стаття, опублікована в листопаді 1996
@uk
مقالة علمية (نشرت في 8-11-1996)
@ar
name
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@ast
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@en
type
label
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@ast
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@en
prefLabel
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@ast
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@en
P2093
P921
P3181
P356
P1476
ATPase activity of the cystic fibrosis transmembrane conductance regulator
@en
P2093
C. E. Bear
J. M. Rommens
M. Ramjeesingh
P304
28463–28468
P3181
P356
10.1074/JBC.271.45.28463
P407
P577
1996-11-08T00:00:00Z