Associated Papers
ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTR.
Wang G
Research Square, 2024
Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.
Soya N et al.
Nature Communications, 2023
CFTR Folding: From Structure and Proteostasis to Cystic Fibrosis Personalized Medicine.
McDonald EF et al.
Acs Chemical Biology, 2023
Acting on the CFTR Membrane-Spanning Domains Interface Rescues Some Misfolded Mutants.
Baatallah N et al.
International Journal of Molecular Sciences, 2022
Nanomechanics combined with HDX reveals allosteric drug binding sites of CFTR NBD1.
Padányi R et al.
Computational and Structural Biotechnology Journal, 2022
A pathogenic role for cystic fibrosis transmembrane conductance regulator in celiac disease.
Villella VR et al.
The Embo Journal, 2019
Differential Scanning Fluorimetry and Hydrogen Deuterium Exchange Mass Spectrometry to Monitor the Conformational Dynamics of NBD1 in Cystic Fibrosis.
Soya N et al.
Methods in Molecular Biology (clifton, N.j.), 2019
Structure-guided combination therapy to potently improve the function of mutant CFTRs.
Veit G et al.
Nature Medicine, 2018
Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.
Bagdany M et al.
Nature Communications, 2017
Molecular modelling and molecular dynamics of CFTR.
Callebaut I et al.
Cellular and Molecular Life Sciences : Cmls, 2017
Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.
Estácio SG et al.
Molecular Biosystems, 2016
Binding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategy.
Hall JD et al.
Protein Science : a Publication of the Protein Society, 2016
Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.
Gong X et al.
The Journal of Biological Chemistry, 2016
On the structural organization of the intracellular domains of CFTR.
Moran O
The International Journal of Biochemistry & Cell Biology, 2014
Synergy-based small-molecule screen using a human lung epithelial cell line yields ΔF508-CFTR correctors that augment VX-809 maximal efficacy.
Phuan PW et al.
Molecular Pharmacology, 2014
Revertant mutants modify, but do not rescue, the gating defect of the cystic fibrosis mutant G551D-CFTR.
Xu Z et al.
The Journal of Physiology, 2014
VX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulator protein through action on membrane-spanning domain 1.
Ren HY et al.
Molecular Biology of the Cell, 2013
Mechanism-based corrector combination restores ΔF508-CFTR folding and function.
Okiyoneda T et al.
Nature Chemical Biology, 2013
Cystic fibrosis transmembrane conductance regulator (ABCC7) structure.
Hunt JF et al.
Cold Spring Harbor Perspectives in Medicine, 2013
Novel pharmacological strategies to treat cystic fibrosis.
Hanrahan JW et al.
Trends in Pharmacological Sciences, 2013
Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.
Rabeh WM et al.
Cell, 2012
Cystic fibrosis: CFTR correctors to the rescue.
Sheppard DN
Chemistry & Biology, 2011
NMR spectroscopy to study the dynamics and interactions of CFTR.
Kanelis V et al.
Methods in Molecular Biology (clifton, N.j.), 2011
Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.
Protasevich I et al.
Protein Science : a Publication of the Protein Society, 2010
Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.
Wang C et al.
Protein Science : a Publication of the Protein Society, 2010
Folding and rescue of a cystic fibrosis transmembrane conductance regulator trafficking mutant identified using human-murine chimeric proteins.
Da Paula AC et al.
The Journal of Biological Chemistry, 2010
Peripheral protein quality control removes unfolded CFTR from the plasma membrane.
Okiyoneda T et al.
Science (new York, N.y.), 2010
Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant.
Atwell S et al.
Protein Engineering, Design & Selection : Peds, 2010
Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.
Lewis HA et al.
Journal of Molecular Biology, 2010
NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.
Kanelis V et al.
The Embo Journal, 2010
Molecular dynamics analysis of the wild type and dF508 mutant structures of the human CFTR-nucleotide binding domain 1.
Bisignano P et al.
Biochimie, 2010
Cooperative assembly and misfolding of CFTR domains in vivo.
Du K et al.
Molecular Biology of the Cell, 2009
Molecular basis for the ATPase activity of CFTR.
Cheung JC et al.
Archives of Biochemistry and Biophysics, 2008
Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces.
Mornon JP et al.
Cellular and Molecular Life Sciences : Cmls, 2008
Defining the defect in F508 del CFTR: a soluble problem?
Deber CM et al.
Chemistry & Biology, 2008
Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation.
Pissarra LS et al.
Chemistry & Biology, 2008
Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure.
Lewis HA et al.
The Journal of Biological Chemistry, 2005
Side chain and backbone contributions of Phe508 to CFTR folding.
Thibodeau PH et al.
Nature Structural & Molecular Biology, 2005
Development and characterization of synthetic antibodies binding to the cystic fibrosis conductance regulator.
Gakhal AK et al.
Mabs, 0