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

Single-molecule dissection of CFTR folding defects and pharmacological rescue.

Proceedings of the National Academy of Sciences of the United States of America - 7 Apr 2026

Kim Sang Ah, Levring Jesper, Chen Jue, Yoon Tae-Young

Abstract excerpt

Cystic fibrosis is a lethal genetic disorder caused by misfolding of the cystic fibrosis transmembrane conductance regulator (CFTR) protein, most commonly due to the ΔF508 mutation. Despite extensive study, CFTR's folding process has remained inaccessible to direct observation. Here, we apply single-molecule magnetic tweezers to resolve the complete folding trajectories of wild-type and ΔF508 CFTR with near-amino...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Cystic Fibrosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to CFTR gene

Share to Mutation

Share to Protein Folding

Share to Single Molecule Imaging

Source

Open in PubMed Open full text

Identifiers

PMID: 41915736
DOI: 10.1073/pnas.2528216123
PMCID: PMC13056111

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-molecule dissection of CFTR folding defects and pharmacological rescue.PMID 41915736Read ↗

Single-molecule dissection of CFTR folding defects and pharmacological rescueSemantic proximity Read ↗

Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Semantic proximity Read ↗

Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR.Semantic proximity Read ↗

Mechanism of dual pharmacological correction and potentiation of human CFTRSemantic proximity Read ↗

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

CFTR function, pathology and pharmacology at single-molecule resolutionSemantic proximity Read ↗

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

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelSemantic proximity Read ↗

Rational coupled dynamics network manipulation rescues disease-relevant mutant cystic fibrosis transmembrane conductance regulatorSemantic proximity Read ↗

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelSemantic proximity Read ↗

A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing MutationSemantic proximity Read ↗

CFTR Folding: From Structure and Proteostasis to Cystic Fibrosis Personalized Medicine.Semantic proximity Read ↗

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