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

Proteasome-dependent pharmacological rescue of cystic fibrosis transmembrane conductance regulator revealed by mutation of glycine 622.

The Journal of pharmacology and experimental therapeutics - 1 Apr 2008

Norez Caroline, Bilan Frédéric, Kitzis Alain, Mettey Yvette, Becq Frédéric

Abstract excerpt

The most common mutation (F508del) causing cystic fibrosis (CF) results in misfolding of the CF transmembrane conductance regulator (CFTR), leading to its degradation via the proteasome pathway. To study the mechanism of action of several pharmacological chaperones benzo[c]quinolizinium (MPB), we analyzed their effects on two CF mutations; F508del-CFTR and G622D-CFTR. The replacement of Gly622 by an aspartic acid...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to Glycine

Share to Mutation

Share to Proteasome Endopeptidase Complex

Share to Protein Transport

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 18230692
DOI: 10.1124/jpet.107.134502

Genes

CFTR

Variants

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteasome-dependent pharmacological rescue of cystic fibrosis transmembrane conductance regulator revealed by mutation of glycine 622.PMID 18230692Read ↗

Therapeutic approaches to CFTR dysfunction: From discovery to drug development.Semantic proximity Read ↗

Regulation of CFTR Biogenesis by the Proteostatic Network and Pharmacological Modulators.Semantic proximity Read ↗

Type I, II, III, IV, and V cystic fibrosis transmembrane conductance regulator defects and opportunities for therapy.Semantic proximity Read ↗

Chemical rescue of deltaF508-CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells.Semantic proximity Read ↗

Transcriptomic and Proteostasis Networks of CFTR and the Development of Small Molecule Modulators for the Treatment of Cystic Fibrosis Lung Disease.Semantic proximity Read ↗

Distinct proteostasis states drive pharmacologic chaperone susceptibility for cystic fibrosis transmembrane conductance regulator misfolding mutants.Semantic proximity Read ↗

Distinct proteostasis states drive pharmacologic chaperone susceptibility for Cystic Fibrosis Transmembrane Conductance Regulator misfolding mutantsSemantic 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 ↗

Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epitheliaSemantic proximity Read ↗

Functional rescue of c.3846G>A (W1282X) in patient-derived nasal cultures achieved by inhibition of nonsense mediated decay and protein modulators with complementary mechanisms of actionSemantic proximity Read ↗

Phosphorylation of the Chaperone-Like HspB5 Rescues Trafficking and Function of F508del-CFTR.Semantic proximity Read ↗

Matrine modulates HSC70 levels and rescues ΔF508-CFTR.Semantic proximity Read ↗

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