Associated Papers
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
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
On the structural organization of the intracellular domains of CFTR.
Moran O
The International Journal of Biochemistry & Cell Biology, 2014
Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.
Rabeh WM et al.
Cell, 2012
State-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3.
Wang G
The Journal of Biological Chemistry, 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
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
Molecular basis for the ATPase activity of CFTR.
Cheung JC et al.
Archives of Biochemistry and Biophysics, 2008
Defining the defect in F508 del CFTR: a soluble problem?
Deber CM et al.
Chemistry & Biology, 2008
Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site.
Ramaen O et al.
Journal of Molecular Biology, 2006
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
PKC-mediated stimulation of amphibian CFTR depends on a single phosphorylation consensus site. insertion of this site confers PKC sensitivity to human CFTR.
Button B et al.
The Journal of General Physiology, 2001