Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.
about
The ABC protein turned chloride channel whose failure causes cystic fibrosisCFTR gating II: Effects of nucleotide binding on the stability of open statesStrict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.Complement yourself: Transcomplementation rescues partially folded mutant proteins.Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Direct effects of 9-anthracene compounds on cystic fibrosis transmembrane conductance regulator gating.A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels.An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening.Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingCysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution.Identification of a novel post-hydrolytic state in CFTR gating.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 defectsInsight in eukaryotic ABC transporter function by mutation analysis.On the mechanism of MgATP-dependent gating of CFTR Cl- channelsReversible silencing of CFTR chloride channels by glutathionylation.Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.The CFTR ion channel: gating, regulation, and anion permeationVx-770 potentiates CFTR function by promoting decoupling between the gating cycle and ATP hydrolysis cycle.A mutation in CFTR modifies the effects of the adenylate kinase inhibitor Ap5A on channel gating.A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.CLC-0 and CFTR: chloride channels evolved from transporters.State-dependent modulation of CFTR gating by pyrophosphate.Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator.A truncated CFTR protein rescues endogenous DeltaF508-CFTR and corrects chloride transport in mice.Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.Conformational changes opening and closing the CFTR chloride channel: insights from cysteine scanning mutagenesis.Degenerate ABC composite site is stably glued together by trapped ATP.High affinity ATP/ADP analogues as new tools for studying CFTR gating.Control of the CFTR channel's gatesThe two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.Protein kinase A regulates ATP hydrolysis and dimerization by a CFTR (cystic fibrosis transmembrane conductance regulator) domain.The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.Calcium activation of ryanodine receptor channels--reconciling RyR gating models with tetrameric channel structureCFTR: an ion channel with a transporter-type energy-coupling mechanism.State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of the cystic fibrosis transmembrane conductance regulator.Mechanism of G551D-CFTR (cystic fibrosis transmembrane conductance regulator) potentiation by a high affinity ATP analog.
P2860
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P2860
Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.
description
2002 nî lūn-bûn
@nan
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
2002年论文
@zh
2002年论文
@zh-cn
name
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@en
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@nl
type
label
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@en
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@nl
prefLabel
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@en
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@nl
P2093
P2860
P1476
Mutation of Walker-A lysine 46 ...... ts nucleotide-binding domains.
@en
P2093
Allan C Powe
Layla Al-Nakkash
Tzyh-Chang Hwang
P2860
P304
P356
10.1113/JPHYSIOL.2001.013162
P407
P577
2002-03-01T00:00:00Z