High affinity ATP/ADP analogues as new tools for studying CFTR gating.
about
Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channelPotentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels.CFTR interacts with ZO-1 to regulate tight junction assembly and epithelial differentiation through the ZONAB pathway.On the mechanism of CFTR inhibition by a thiazolidinone derivative.Identification of a novel post-hydrolytic state in CFTR gating.G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defectsThe CFTR ion channel: gating, regulation, and anion permeationThree-dimensional reconstruction of human cystic fibrosis transmembrane conductance regulator chloride channel revealed an ellipsoidal structure with orifices beneath the putative transmembrane domainConformational changes in the catalytically inactive nucleotide-binding site of CFTR.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.Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approachGating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.2-MeS-beta,gamma-CCl2-ATP is a potent agent for reducing intraocular pressureOn the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator.Degenerate ABC composite site is stably glued together by trapped ATP.The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.State-dependent inhibition of cystic fibrosis transmembrane conductance regulator chloride channels by a novel peptide toxin.Mechanism of G551D-CFTR (cystic fibrosis transmembrane conductance regulator) potentiation by a high affinity ATP analog.CFTR potentiators: from bench to bedside.A common mechanism for CFTR potentiators.Structural mechanisms of CFTR function and dysfunction.
P2860
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P2860
High affinity ATP/ADP analogues as new tools for studying CFTR gating.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
High affinity ATP/ADP analogues as new tools for studying CFTR gating.
@en
type
label
High affinity ATP/ADP analogues as new tools for studying CFTR gating.
@en
prefLabel
High affinity ATP/ADP analogues as new tools for studying CFTR gating.
@en
P2093
P2860
P1476
High affinity ATP/ADP analogues as new tools for studying CFTR gating.
@en
P2093
Tzyh-Chang Hwang
Xiaohui Wang
Xiaoqin Zou
Yoshiro Sohma
P2860
P304
P356
10.1113/JPHYSIOL.2005.095083
P407
P577
2005-10-13T00:00:00Z