Side chain and backbone contributions of Phe508 to CFTR folding.
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Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisDeletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperoneThe ABC protein turned chloride channel whose failure causes cystic fibrosisProtein folding: then and nowThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyStructures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutantThe Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): THREE-DIMENSIONAL STRUCTURE AND LOCALIZATION OF A CHANNEL GATERequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesDiminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfoldingThe primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domainThe silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunctionThe endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function.New insights into interactions between the nucleotide-binding domain of CFTR and keratin 8.Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Codon bias and the folding dynamics of the cystic fibrosis transmembrane conductance regulator.Development of CFTR StructureSmall molecule correctors of F508del-CFTR discovered by structure-based virtual screeningCFTR is a negative regulator of NFkappaB mediated innate immune response.Interplay between ER exit code and domain conformation in CFTR misprocessing and rescue.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexinDecoding F508del misfolding in cystic fibrosis.Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.A chaperone trap contributes to the onset of cystic fibrosis.Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingThe NF-kappaB signaling in cystic fibrosis lung disease: pathophysiology and therapeutic potentialRegulation of ABCC6 trafficking and stability by a conserved C-terminal PDZ-like sequenceCorrection of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809.Alteration of CFTR transmembrane span integration by disease-causing mutations.Small heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation.Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signalDevelopment and characterization of synthetic antibodies binding to the cystic fibrosis conductance regulator.Molecular modelling and molecular dynamics of CFTR.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Update in cystic fibrosis 2005Channel Gating Regulation by the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) First Cytosolic Loop.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
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Side chain and backbone contributions of Phe508 to CFTR folding.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Side chain and backbone contributions of Phe508 to CFTR folding.
@ast
Side chain and backbone contributions of Phe508 to CFTR folding.
@en
type
label
Side chain and backbone contributions of Phe508 to CFTR folding.
@ast
Side chain and backbone contributions of Phe508 to CFTR folding.
@en
prefLabel
Side chain and backbone contributions of Phe508 to CFTR folding.
@ast
Side chain and backbone contributions of Phe508 to CFTR folding.
@en
P2860
P356
P1476
Side chain and backbone contributions of Phe508 to CFTR folding.
@en
P2093
Patrick H Thibodeau
Philip J Thomas
P2860
P2888
P356
10.1038/NSMB881
P577
2004-12-26T00:00:00Z