about
A novel host defense system of airways is defective in cystic fibrosisRequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesRelationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel poreDual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Discovery of glycine hydrazide pore-occluding CFTR inhibitors: mechanism, structure-activity analysis, and in vivo efficacy.The block of CFTR by scorpion venom is state-dependentCystic fibrosis transmembrane conductance regulator chloride channel blockers: Pharmacological, biophysical and physiological relevance.Nanomolar CFTR inhibition by pore-occluding divalent polyethylene glycol-malonic acid hydrazidesDivergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, glibenclamide, and GlyH-101Murine and human CFTR exhibit different sensitivities to CFTR potentiators.Voltage-dependent gating of the cystic fibrosis transmembrane conductance regulator Cl- channel.CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.Transcomplementation by a truncation mutant of cystic fibrosis transmembrane conductance regulator (CFTR) enhances ΔF508 processing through a biomolecular interactionMutations at arginine 352 alter the pore architecture of CFTR.Enteric oxalate secretion is not directly mediated by the human CFTR chloride channel.Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore.Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel.On the origin of asymmetric interactions between permeant anions and the cystic fibrosis transmembrane conductance regulator chloride channel pore.Introduction to section IV: biophysical methods to approach CFTR structure.Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore.A synthetic prostone activates apical chloride channels in A6 epithelial cells.Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel.Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Permeation through the CFTR chloride channel.
@ast
Permeation through the CFTR chloride channel.
@en
type
label
Permeation through the CFTR chloride channel.
@ast
Permeation through the CFTR chloride channel.
@en
prefLabel
Permeation through the CFTR chloride channel.
@ast
Permeation through the CFTR chloride channel.
@en
P1476
Permeation through the CFTR chloride channel.
@en
P2093
McCarty NA
P304
P577
2000-07-01T00:00:00Z