Solubilizing Mutations Used to Crystallize One CFTR Domain Attenuate the Trafficking and Channel Defects Caused by the Major Cystic Fibrosis Mutation
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Mechanisms of CFTR Folding at the Endoplasmic ReticulumDeletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperoneRequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesAllosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTRThe endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Deletion of CFTR translation start site reveals functional isoforms of the protein in CF patients.Folding and rescue of a cystic fibrosis transmembrane conductance regulator trafficking mutant identified using human-murine chimeric proteinsInterplay between ER exit code and domain conformation in CFTR misprocessing and rescue.Decoding F508del misfolding in cystic fibrosis.Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.VX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulator protein through action on membrane-spanning domain 1.Association of cystic fibrosis transmembrane conductance regulator gene variants with acute lung injury in African American children with pneumonia*.Detection of phospho-sites generated by protein kinase CK2 in CFTR: mechanistic aspects of Thr1471 phosphorylationHuman-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activityDeletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.Restoration of NBD1 thermal stability is necessary and sufficient to correct ∆F508 CFTR folding and assemblyBinding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategyCFTR: folding, misfolding and correcting the ΔF508 conformational defect.Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR traffickingTargeting F508del-CFTR to develop rational new therapies for cystic fibrosis.Cystic fibrosis transmembrane conductance regulator (ABCC7) structureFrom the endoplasmic reticulum to the plasma membrane: mechanisms of CFTR folding and trafficking.Revertant mutants modify, but do not rescue, the gating defect of the cystic fibrosis mutant G551D-CFTR.Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTRThe most common cystic fibrosis-associated mutation destabilizes the dimeric state of the nucleotide-binding domains of CFTR.Biochemical and biophysical approaches to probe CFTR structure.Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator.Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.
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P2860
Solubilizing Mutations Used to Crystallize One CFTR Domain Attenuate the Trafficking and Channel Defects Caused by the Major Cystic Fibrosis Mutation
description
scientific article published on 01 January 2008
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 2008
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name
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
@en
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
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type
label
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
@en
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
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prefLabel
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
@en
Solubilizing Mutations Used to ...... Major Cystic Fibrosis Mutation
@nl
P2093
P50
P1476
Solubilizing mutations used to ...... major cystic fibrosis mutation
@en
P2093
André Schmidt
David N Sheppard
Luísa S Pissarra
Philip J Thomas
Zhiwei Cai
P356
10.1016/J.CHEMBIOL.2007.11.012
P577
2008-01-01T00:00:00Z