Article

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channel

2025-10-08

Abstract excerpt

<h4>SUMMARY</h4> Defects in protein trafficking underlie many genetic diseases, including cystic fibrosis (CF), where the predominant F508del mutation destabilizes the cystic fibrosis transmembrane conductance regulator (CFTR) channel, leading to its degradation. To provide a protein-specific chaperone, we used lipid nanoparticles to deliver mRNA encoding T2a, a nanobody that thermally stabilizes CFTR via high-af...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 9d1115fb-abd1-5baf-aac3-357bc1b333e4
DOI: 10.1101/2025.10.08.681081

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelDOI 10.1101/2025.10.08.681081Read

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

Domain-interface dynamics of CFTR revealed by stabilizing nanobodiesSemantic proximity Read

Mechanism of CFTR correction by type I folding correctorsSemantic proximity Read

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

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

A Cell-Permeable Nanobody to Restore F508del Cystic Fibrosis Transmembrane Conductance Regulator ActivitySemantic proximity Read

Rescue of F508del CFTR: Commentary on "F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive".Semantic proximity Read

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

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

The CFTR P67L variant reveals a key role for N-terminal lasso helices in channel folding, maturation, and pharmacologic rescue.Semantic proximity Read

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

Structural stability of purified human CFTR is systematically improved by mutations in nucleotide binding domain 1.Semantic proximity Read