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

A chemical corrector modifies the channel function of F508del-CFTR.

Molecular pharmacology - 1 Sept 2010

Kim Chiaw Patrick, Wellhauser Leigh, Huan Ling Jun, Ramjeesingh Mohabir, Bear Christine E

Abstract excerpt

The deletion of Phe-508 (F508del) constitutes the most prevalent cystic fibrosis-causing mutation. This mutation leads to cystic fibrosis transmembrane conductance regulator (CFTR) misfolding and retention in the endoplasmic reticulum and altered channel activity in mammalian cells. This folding...

Read the complete abstract on PubMed

Topics

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

Share to Cricetinae
Share to Cystic Fibrosis
Share to Cystic Fibrosis Transmembrane Conductance Regulator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to Phenylalanine

Share to Piperazines

Share to Protein Transport

Share to Quinazolines

Source

Identifiers

PMID: 20501743
DOI: 10.1124/mol.110.065862

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20501743-2026-09-02.2. 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

A chemical corrector modifies the channel function of F508del-CFTR.PMID 20501743Read ↗

Functional Rescue of F508del-CFTR Using Small Molecule CorrectorsSemantic proximity Read ↗

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

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

Identification of novel F508del-CFTR traffic correctors among triazole derivatives.Semantic proximity Read ↗

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

A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability.Semantic proximity Read ↗

Rescue of the mutant CFTR chloride channel by pharmacological correctors and low temperature analyzed by gene expression profiling.Semantic proximity Read ↗

Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Semantic proximity Read ↗

Rescuing mutant CFTR: a multi-task approach to a better outcome in treating cystic fibrosis.Semantic proximity Read ↗

Rescue of folding defects in ABC transporters using pharmacological chaperones.Semantic proximity Read ↗

Novel tricyclic pyrrolo-quinolines as pharmacological correctors of the mutant CFTR chloride channel.Semantic proximity Read ↗

Partial rescue of F508del‐cystic fibrosis transmembrane conductance regulator channel gating with modest improvement of protein processing, but not stability, by a dual‐acting small moleculeSemantic proximity Read ↗

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