Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Correcting temperature-sensitive protein folding defects.

The Journal of clinical investigation - 15 Mar 1997

Brown C R, Hong-Brown L Q, Welch W J

Abstract excerpt

Recently, we found that different low molecular weight compounds, all known to stabilize proteins in their native conformation, are effective in correcting the temperature-sensitive protein folding defect associated with the deltaF508 cystic fibrosis transmembrane regulator (CFTR) protein. Here w...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Mutation
Share to Protein Folding
Share to Rats

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Temperature

Share to Cell Line

Share to CFTR gene

Share to Ligases

Share to Tumor Suppressor Protein p53

Source

Open in PubMed Open full text

Identifiers

PMID: 9077553
DOI: 10.1172/JCI119302
PMCID: PMC507959

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9077553-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

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

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Correcting temperature-sensitive protein folding defects.PMID 9077553Read ↗

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

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

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

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

Mechanism of CFTR correction by type I folding correctors.Semantic proximity Read ↗

Therapeutic approaches to repair defects in deltaF508 CFTR folding and cellular targeting.Semantic proximity Read ↗

Corrector-mediated rescue of misprocessed CFTR mutants can be reduced by the P-glycoprotein drug pump.Semantic proximity Read ↗

Combination of Correctors Rescue ΔF508-CFTR by Reducing Its Association with Hsp40 and Hsp27.Semantic proximity Read ↗

A chemical corrector modifies the channel function of F508del-CFTR.Semantic proximity Read ↗

Mechanism of CFTR correction by type I folding correctorsSemantic proximity Read ↗

Pharmacological chaperones: a new twist on receptor folding.Semantic proximity Read ↗

Therapy through chaperones: sense or antisense? Cystic fibrosis as a model disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.