Structure, gating, and regulation of the CFTR anion channel
The cystic fibrosis transmembrane conductance regulator (CFTR) belongs to the ATP
binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for …
binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for …
The ABC protein turned chloride channel whose failure causes cystic fibrosis
CFTR chloride channels are encoded by the gene mutated in patients with cystic fibrosis.
These channels belong to the superfamily of ABC transporter ATPases. ATP-driven …
These channels belong to the superfamily of ABC transporter ATPases. ATP-driven …
[HTML][HTML] Atomic structure of the cystic fibrosis transmembrane conductance regulator
The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel
evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined …
evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined …
[HTML][HTML] Structural biology of bacterial iron uptake
KD Krewulak, HJ Vogel - Biochimica et Biophysica Acta (BBA) …, 2008 - Elsevier
To fulfill their nutritional requirement for iron, bacteria utilize various iron sources which
include the host proteins transferrin and lactoferrin, heme, and low molecular weight iron …
include the host proteins transferrin and lactoferrin, heme, and low molecular weight iron …
CFTR function and prospects for therapy
JR Riordan - Annu. Rev. Biochem., 2008 - annualreviews.org
Mutations in the gene coding for the cystic fibrosis transmembrane conductance regulator
(CFTR) epithelial anion channel cause cystic fibrosis (CF). The multidomain integral …
(CFTR) epithelial anion channel cause cystic fibrosis (CF). The multidomain integral …
Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
The pathways that distinguish transport of folded and misfolded cargo through the exocytic
(secretory) pathway of eukaryotic cells remain unknown. Using proteomics to assess global …
(secretory) pathway of eukaryotic cells remain unknown. Using proteomics to assess global …
[HTML][HTML] Requirements for efficient correction of ΔF508 CFTR revealed by analyses of evolved sequences
JL Mendoza, A Schmidt, Q Li, E Nuvaga, T Barrett… - Cell, 2012 - cell.com
Misfolding of ΔF508 cystic fibrosis (CF) transmembrane conductance regulator (CFTR)
underlies pathology in most CF patients. F508 resides in the first nucleotide-binding domain …
underlies pathology in most CF patients. F508 resides in the first nucleotide-binding domain …
Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
M Hohl, C Briand, MG Grütter, MA Seeger - Nature structural & …, 2012 - nature.com
ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell
membranes by alternating between inward-and outward-facing conformations, harnessing …
membranes by alternating between inward-and outward-facing conformations, harnessing …
The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
Misfolding accounts for the endoplasmic reticulum–associated degradation of mutant cystic
fibrosis transmembrane conductance regulators (CFTRs), including deletion of Phe508 …
fibrosis transmembrane conductance regulators (CFTRs), including deletion of Phe508 …
Phenylalanine-508 mediates a cytoplasmic–membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
AWR Serohijos, T Hegedűs… - Proceedings of the …, 2008 - National Acad Sciences
Deletion of phenylalanine-508 (Phe-508) from the N-terminal nucleotide-binding domain
(NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR), a member of the …
(NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR), a member of the …