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Article

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.

PLoS computational biology - 29 Feb 2008

Serohijos Adrian W R, Hegedus Tamás, Riordan John R, Dokholyan Nikolay V

Abstract excerpt

The absence of a functional ATP Binding Cassette (ABC) protein called the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) from apical membranes of epithelial cells is responsible for cystic fibrosis (CF). Over 90% of CF patients carry at least one mutant allele with deletion of phenylalanine at position 508 located in the N-terminal nucleotide binding domain (NBD1). Biochemical and cell biological...

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Source

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Identifiers

PMID: 18463704
DOI: 10.1371/journal.pcbi.1000008
PMCID: PMC2265529

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

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.PMID 18463704Read ↗

Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Semantic proximity Read ↗

Cystic fibrosis: a disease of altered protein folding.Semantic proximity Read ↗

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

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

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

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

Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Semantic proximity Read ↗

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

A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing MutationSemantic proximity Read ↗

Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR.Semantic proximity Read ↗

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.Semantic proximity Read ↗

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