Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.
about
Impact of the F508del mutation on ovine CFTR, a Cl- channel with enhanced conductance and ATP-dependent gating.Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.Cystic fibrosis transmembrane conductance regulator chloride channel blockers: Pharmacological, biophysical and physiological relevance.An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening.Modeling the conformational changes underlying channel opening in CFTRLocalizing a gate in CFTR.Mechanisms of CFTR functional variants that impair regulated bicarbonate permeation and increase risk for pancreatitis but not for cystic fibrosis.Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.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.The CFTR ion channel: gating, regulation, and anion permeationLong-range coupling between the extracellular gates and the intracellular ATP binding domains of multidrug resistance protein pumps and cystic fibrosis transmembrane conductance regulator channelsCysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeationSpatial positioning of CFTR's pore-lining residues affirms an asymmetrical contribution of transmembrane segments to the anion permeation pathwayNonequilibrium gating of CFTR on an equilibrium theme.Functional architecture of the CFTR chloride channel.Metal bridges to probe membrane ion channel structure and function.Cytoplasmic pathway followed by chloride ions to enter the CFTR channel pore.Structural Changes Fundamental to Gating of the Cystic Fibrosis Transmembrane Conductance Regulator Anion Channel Pore.The biophysics, biochemistry and physiology of CFTR.Relative movements of transmembrane regions at the outer mouth of the cystic fibrosis transmembrane conductance regulator channel pore during channel gatingCystic Fibrosis Transmembrane Conductance Regulator (CFTR): CLOSED AND OPEN STATE CHANNEL MODELS.Relative contribution of different transmembrane segments to the CFTR chloride channel pore.Loop diuretics are open-channel blockers of the cystic fibrosis transmembrane conductance regulator with distinct kinetics.A SAXS-based ensemble model of the native and phosphorylated regulatory domain of the CFTR.External Zn(2+) binding to cysteine-substituted cystic fibrosis transmembrane conductance regulator constructs regulates channel gating and curcumin potentiation.Structural mechanisms of CFTR function and dysfunction.
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P2860
Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@ast
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@en
type
label
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@ast
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@en
prefLabel
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@ast
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@en
P2093
P2860
P356
P1433
P1476
Cystic fibrosis transmembrane ...... es a "bottleneck" in the pore.
@en
P2093
Anthony Ivetac
Christopher Alexander
David C Dawson
John Kirkham
Mark S P Sansom
Nicolette O'Donnell
Yohei Norimatsu
P2860
P304
P356
10.1021/BI201888A
P407
P577
2012-03-07T00:00:00Z