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Article

Investigation of F508del CFTR unfolding and a search for stabilizing small molecules.

Archives of biochemistry and biophysics - 1 Aug 2024

Meng Xin, Ford Robert C

Abstract excerpt

Mutation of phenylalanine at position 508 in the cystic fibrosis transmembrane conductance regulator (F508del CFTR) yields a protein unstable at physiological temperatures that is rapidly degraded in the cell. This mutation is present in about 90% of cystic fibrosis patients, hence there is great interest in compounds reversing its instability. We have previously reported the expression of the mutated protein at...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 38876247
DOI: 10.1016/j.abb.2024.110050

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

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Investigation of F508del CFTR unfolding and a search for stabilizing small molecules.PMID 38876247Read ↗

The cystic fibrosis transmembrane conductance regulator (CFTR) and its stabilitySemantic proximity Read ↗

Strategies for correcting the delta F508 CFTR protein-folding defect.Semantic proximity Read ↗

Manipulating the folding pathway of delta F508 CFTR using chemical chaperones.Semantic proximity Read ↗

Two Small Molecules Restore Stability to a Subpopulation of the Cystic Fibrosis Transmembrane Conductance Regulator with the Predominant Disease-causing Mutation.Semantic proximity Read ↗

Evaluation of a systems biology approach to identify pharmacological correctors of the mutant CFTR chloride channel.Semantic proximity Read ↗

Conformational and temperature-sensitive stability defects of the delta F508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments.Semantic proximity Read ↗

Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.Semantic proximity Read ↗

Altered protein folding may be the molecular basis of most cases of cystic fibrosisSemantic proximity Read ↗

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelSemantic proximity Read ↗

Increasing the Endoplasmic Reticulum Pool of the F508del Allele of the Cystic Fibrosis Transmembrane Conductance Regulator Leads to Greater Folding Correction by Small Molecule Therapeutics.Semantic proximity Read ↗

Structural stability of purified human CFTR is systematically improved by mutations in nucleotide binding domain 1.Semantic proximity Read ↗

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.Semantic proximity Read ↗

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