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Article

Cystic fibrosis: a disease of altered protein folding.

Journal of bioenergetics and biomembranes - 1 Oct 1997

Qu B H, Strickland E, Thomas P J

Abstract excerpt

Cystic fibrosis (CF) is caused by mutations in the gene that encodes the cystic fibrosis transmembrane conductance regulator, CFTR. Previously we demonstrated that the common delta F508 mutation in the first nucleotide binding domain (NBD1) alters the ability of the domain to fold into a functional three-dimensional structure, providing a molecular explanation for the observation that the mutant CFTR is retained...

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Source

Identifiers

PMID: 9511933
DOI: 10.1023/a:1022439108101

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cystic fibrosis: a disease of altered protein folding.PMID 9511933Read ↗

CFTR trafficking mutations disrupt cotranslational protein folding by targeting biosynthetic intermediates.Semantic proximity Read ↗

Alteration of the Cystic Fibrosis Transmembrane Conductance Regulator Folding PathwaySemantic proximity Read ↗

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.Semantic proximity Read ↗

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

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.Semantic proximity Read ↗

Structure basis of CFTR folding, function and pharmacology.Semantic proximity Read ↗

Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and StructureSemantic proximity Read ↗

A novel model for the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

CFTR Folding: From Structure and Proteostasis to Cystic Fibrosis Personalized Medicine.Semantic proximity Read ↗

ABC-transporter CFTR folds with high fidelity through a modular, stepwise pathwaySemantic proximity Read ↗

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

CFTR misfolds during native-centric simulations due to entropic penalties of native state formationSemantic proximity Read ↗

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