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Published in 2018 at "Pediatric Pulmonology"
DOI: 10.1002/ppul.24151
Abstract: membrane, but rather undergoes constitutive internalization from the cell surface (1). Indeed, the endocytic kinetics for CFTR are remarkably fast, approaching that of nutrient receptors such as the LDL and transferrin receptors (2-4). Although there…
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Keywords:
cftr;
recycling pathway;
f508 cftr;
cell surface ... See more keywords
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Published in 2018 at "SLAS Discovery"
DOI: 10.1177/2472555218763310
Abstract: The most common cystic fibrosis–causing mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) is deletion of phenylalanine at residue 508 (∆F508). The ∆F508 mutation impairs folding of nucleotide binding domain 1 (NBD1) and interfacial…
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Keywords:
cftr;
cell surface;
f508 cftr;
domain ... See more keywords
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2
Published in 2022 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2022.840649
Abstract: The peripheral protein quality control (periQC) system eliminates the conformationally defective cystic fibrosis transmembrane conductance regulator (CFTR), including ∆F508-CFTR, from the plasma membrane (PM) and limits the efficacy of pharmacological therapy for cystic fibrosis (CF).…
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Keywords:
f508 cftr;
cftr periqc;
rffl;
cftr ... See more keywords
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Published in 2022 at "Nutrients"
DOI: 10.3390/nu14204283
Abstract: Treatment of cystic fibrosis relies so far on expensive and sophisticated drugs. A logical approach to rescuing the defective ΔF508-CFTR protein has not yet been published. Therefore, virtual docking of ATP and CFTR activators to…
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Keywords:
f508 cftr;
cftr;
recovery f508;
citrate ... See more keywords