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

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

Molecular pharmacology - 1 Mar 2007

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

Abstract excerpt

Cystic fibrosis transmembrane conductance regulator (CFTR) and P-glycoprotein (P-gp) are ATP-binding cassette (ABC) transporters that have two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). Defective folding of CFTR lacking phenylalanine 508 (DeltaPhe508) in NBD1 is the most common cause of cystic fibrosis. The Phe508 position seems to be universally important in ABC transporters because...

Read the complete abstract on PubMed

Topics

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

Share to ATP Binding Cassette Transporter, Subfamily B, Member 1
Share to Cystic Fibrosis Transmembrane Conductance Regulator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Molecular Chaperones

Share to Piperazines

Share to Protein Folding

Share to Protein Structure, Tertiary

Share to Quinazolines

Source

Identifiers

PMID: 17132688
DOI: 10.1124/mol.106.029926

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones.PMID 17132688Read ↗

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

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

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

The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.Semantic proximity Read ↗

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

Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR).Semantic proximity Read ↗

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

Corrector VX-809 stabilizes the first transmembrane domain of CFTR.Semantic proximity Read ↗

Introduction of the most common cystic fibrosis mutation (Delta F508) into human P-glycoprotein disrupts packing of the transmembrane segments.Semantic proximity Read ↗

Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains.Semantic proximity Read ↗

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

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

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