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Article

Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation.

The Journal of biological chemistry - 12 Jan 1996

Sato S, Ward C L, Krouse M E, Wine J J, Kopito R R

Abstract excerpt

The common delta F508 mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) interferes with the biosynthetic folding of nascent CFTR polypeptides, leading to their retention and rapid degradation in an intracellular compartment proximal to the Golgi apparatus. Neither the pathway by which wild-type CFTR folds nor the mechanism by which the Phe508 deletion interferes with this process is well...

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Source

Identifiers

PMID: 8557666
DOI: 10.1074/jbc.271.2.635

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation.PMID 8557666Read ↗

CFTR: folding, misfolding and correcting the ΔF508 conformational defect.Semantic proximity Read ↗

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

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

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

The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment.Semantic proximity Read ↗

Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

Misassembled mutant DeltaF508 CFTR in the distal secretory pathway alters cellular lipid trafficking.Semantic proximity Read ↗

Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin.Semantic proximity Read ↗

CFTR and chaperones: processing and degradation.Semantic proximity Read ↗

The cystic-fibrosis-associated ΔF508 mutation confers post-transcriptional destabilization on the C. elegans ABC transporter PGP-3.Semantic proximity Read ↗

Defects in processing and trafficking of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

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