Molecular models of the open and closed states of the whole human CFTR protein.
about
Integrated analysis of residue coevolution and protein structure in ABC transportersThe Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): THREE-DIMENSIONAL STRUCTURE AND LOCALIZATION OF A CHANNEL GATEThe primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domainGenome-wide Membrane Protein Structure Prediction.Impact of the F508del mutation on ovine CFTR, a Cl- channel with enhanced conductance and ATP-dependent gating.The cystic fibrosis transmembrane conductance regulator (CFTR) and its stabilityDevelopment of CFTR StructureMissense mutations in the ABCB6 transporter cause dominant familial pseudohyperkalemia.ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions.Alteration of protein function by a silent polymorphism linked to tRNA abundance.Decoding F508del misfolding in cystic fibrosis.Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR.Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.A chaperone trap contributes to the onset of cystic fibrosis.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.CFTR inhibitors.Modeling the conformational changes underlying channel opening in CFTRProbing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Phenotype-optimized sequence ensembles substantially improve prediction of disease-causing mutation in 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.Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Pharmacological rescue of the mutant cystic fibrosis transmembrane conductance regulator (CFTR) detected by use of a novel fluorescence platformMolecular modelling and molecular dynamics of CFTR.Cystic fibrosis lung environment and Pseudomonas aeruginosa infection.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 permeationCorrectors of ΔF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein.Long-range coupling between the extracellular gates and the intracellular ATP binding domains of multidrug resistance protein pumps and cystic fibrosis transmembrane conductance regulator channelsRestoration of NBD1 thermal stability is necessary and sufficient to correct ∆F508 CFTR folding and assemblyCysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeationDynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stabilityCFTR: folding, misfolding and correcting the ΔF508 conformational defect.Converting nonhydrolyzable nucleotides to strong cystic fibrosis transmembrane conductance regulator (CFTR) agonists by gain of function (GOF) mutationsTwo salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.Targeting F508del-CFTR to develop rational new therapies for cystic fibrosis.
P2860
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P2860
Molecular models of the open and closed states of the whole human CFTR protein.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Molecular models of the open and closed states of the whole human CFTR protein.
@en
Molecular models of the open and closed states of the whole human CFTR protein.
@nl
type
label
Molecular models of the open and closed states of the whole human CFTR protein.
@en
Molecular models of the open and closed states of the whole human CFTR protein.
@nl
prefLabel
Molecular models of the open and closed states of the whole human CFTR protein.
@en
Molecular models of the open and closed states of the whole human CFTR protein.
@nl
P2093
P1476
Molecular models of the open and closed states of the whole human CFTR protein.
@en
P2093
Isabelle Callebaut
Jean-Paul Mornon
Pierre Lehn
P2888
P304
P356
10.1007/S00018-009-0133-0
P577
2009-08-26T00:00:00Z