Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the pore
about
Anion transport in heartRelationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel poreMouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA-regulated apical chloride channels in cortical collecting ductMouse bestrophin-2 is a bona fide Cl(-) channel: identification of a residue important in anion binding and conduction.Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator.CFTR: a cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore.CFTR: Ligand exchange between a permeant anion ([Au(CN)2]-) and an engineered cysteine (T338C) blocks the pore.Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Divergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, glibenclamide, and GlyH-101Insight in eukaryotic ABC transporter function by mutation analysis.Transmembrane helical interactions in the CFTR channel pore.Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.Probing an open CFTR pore with organic anion blockersCystic fibrosis transmembrane conductance regulator. Physical basis for lyotropic anion selectivity patternsAnion permeation in Ca(2+)-activated Cl(-) channels.CFTR: covalent modification of cysteine-substituted channels expressed in Xenopus oocytes shows that activation is due to the opening of channels resident in the plasma membraneCFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.Cystic fibrosis transmembrane conductance regulator (ABCC7) structureOn the origin of asymmetric interactions between permeant anions and the cystic fibrosis transmembrane conductance regulator chloride channel pore.Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl- channel expressed in mammalian cell lines.Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore.Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel.Structural and ionic determinants of 5-nitro-2-(3-phenylprophyl-amino)-benzoic acid block of the CFTR chloride channel.Identification of a region of strong discrimination in the pore of CFTR.Cooperativity and flexibility of cystic fibrosis transmembrane conductance regulator transmembrane segments participate in membrane localization of a charged residue.Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore.Inhibition of CFTR channels by a peptide toxin of scorpion venom.Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating.Voltage-sensitive gating induced by a mutation in the fifth transmembrane domain of CFTR.Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge.Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis.Anions permeate and gate GCAC1, a voltage-dependent guard cell anion channel
P2860
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P2860
Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the pore
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@ast
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@en
type
label
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@ast
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@en
prefLabel
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@ast
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@en
P2093
P2860
P1433
P1476
Cystic fibrosis transmembrane ...... binding as a probe of the pore
@en
P2093
D C Dawson
F S Collins
M K Mansoura
N W Richards
T V Strong
P2860
P304
P356
10.1016/S0006-3495(98)77845-2
P407
P577
1998-03-01T00:00:00Z