Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
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CFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).A cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gatingTRPM7Cystic fibrosis transmembrane conductance regulator gating requires cytosolic electrolytes.Perturbation of the pore of the cystic fibrosis transmembrane conductance regulator (CFTR) inhibits its atpase activity.Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.Electrophysiological evidence for the presence of cystic fibrosis transmembrane conductance regulator (CFTR) in mouse sperm.Cysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels.The block of CFTR by scorpion venom is state-dependentVX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulator protein through action on membrane-spanning domain 1.State-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3.Lumacaftor and ivacaftor in the management of patients with cystic fibrosis: current evidence and future prospects.A conditional probability analysis of cystic fibrosis transmembrane conductance regulator gating indicates that ATP has multiple effects during the gating cycle.Use of chimeric proteins to investigate the role of transporter associated with antigen processing (TAP) structural domains in peptide binding and translocation.On the mechanism of MgATP-dependent gating of CFTR Cl- channelsDistinct Mg(2+)-dependent steps rate limit opening and closing of a single CFTR Cl(-) channel.A mutation in CFTR modifies the effects of the adenylate kinase inhibitor Ap5A on channel gating.State-dependent modulation of CFTR gating by pyrophosphate.Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiologyMutation-specific potency and efficacy of cystic fibrosis transmembrane conductance regulator chloride channel potentiators.Intracellular ATP binding is required to activate the slowly activating K+ channel I(Ks)Cystic fibrosis-related oxidative stress and intestinal lipid disorders.Calcium-modulated chloride pathways contribute to chloride flux in murine cystic fibrosis-affected macrophages.Altering intracellular pH reveals the kinetic basis of intraburst gating in the CFTR Cl- channel.Characterization of mitochondrial function in cells with impaired cystic fibrosis transmembrane conductance regulator (CFTR) function.CFTR directly mediates nucleotide-regulated glutathione flux.Restoration of W1282X CFTR activity by enhanced expression.High affinity ATP/ADP analogues as new tools for studying CFTR gating.4-Chloro-benzo[F]isoquinoline (CBIQ) activates CFTR chloride channels and KCNN4 potassium channels in Calu-3 human airway epithelial cellsFunctional analysis of the C-terminal boundary of the second nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator and structural implications.The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.Cystic fibrosis transmembrane conductance regulator: the NBF1+R (nucleotide-binding fold 1 and regulatory domain) segment acting alone catalyses a Co2+/Mn2+/Mg2+-ATPase activity markedly inhibited by both Cd2+ and the transition-state analogue orthoProtein kinase A regulates ATP hydrolysis and dimerization by a CFTR (cystic fibrosis transmembrane conductance regulator) domain.State-dependent inhibition of cystic fibrosis transmembrane conductance regulator chloride channels by a novel peptide toxin.Direct sensing of intracellular pH by the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channelMutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating.Activation of G551D CFTR channel with MPB-91: regulation by ATPase activity and phosphorylation.Mutations that change the position of the putative gamma-phosphate linker in the nucleotide binding domains of CFTR alter channel gating.The cystic fibrosis mutation G551D alters the non-Michaelis-Menten behavior of the cystic fibrosis transmembrane conductance regulator (CFTR) channel and abolishes the inhibitory Genistein binding site.
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P2860
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on July 2000
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@en
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@nl
type
label
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@en
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@nl
prefLabel
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@en
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@nl
P2860
P356
P1476
Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.
@en
P2093
P2860
P304
P356
10.1073/PNAS.140220597
P407
P577
2000-07-01T00:00:00Z