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Article

Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones.

Molecular pharmacology - 1 Jul 2006

Wang Ying, Bartlett M Claire, Loo Tip W, Clarke David M

Abstract excerpt

Most mutants of the cystic fibrosis transmembrane conductance regulator (CFTR) that cause severe symptoms of cystic fibrosis do not reach the cell surface because they are defective in folding. Many CFTR folding mutants, however, including the DeltaF508 mutant found in more than 90% of cystic fib...

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Source

Identifiers

PMID: 16624886
DOI: 10.1124/mol.106.023994

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16624886-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones.PMID 16624886Read ↗

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Repair of CFTR folding defects with correctors that function as pharmacological chaperones.Semantic proximity Read ↗

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The chemical chaperone CFcor-325 repairs folding defects in the transmembrane domains of CFTR-processing mutants.Semantic proximity Read ↗

Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones.Semantic proximity Read ↗

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Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening.Semantic proximity Read ↗

Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein.Semantic proximity Read ↗

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