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

Defining the defect in F508 del CFTR: a soluble problem?

Chemistry & biology - 1 Jan 2008

Deber Charles M, Cheung Joanne C, Rath Arianna

Abstract excerpt

Previously reported crystal structures of CFTR F508 del-NBD1 were determined in the presence of solubilizing mutations. In this issue of Chemistry & Biology, Pissarra et al. (2008) show that partial rescue of the trafficking and gating defects of full-length CFTR occurs in vivo upon recapitulatio...

Read the complete abstract on PubMed

Topics

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

Share to Biological Factors
Share to Cystic Fibrosis Transmembrane Conductance Regulator
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Nucleotides

Share to Solubility

Share to Solutions

Share to Stereoisomerism

Source

Identifiers

PMID: 18215767
DOI: 10.1016/j.chembiol.2008.01.001

Genes

CFTR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18215767-2026-09-02.2. 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

Defining the defect in F508 del CFTR: a soluble problem?PMID 18215767Read ↗

Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation.Semantic proximity Read ↗

Identification of a NBD1-Binding Pharmacological Chaperone that Corrects the Trafficking Defect of F508del-CFTRSemantic proximity Read ↗

Can two wrongs make a right? F508del-CFTR ion channel rescue by second-site mutations in its transmembrane domains.Semantic proximity Read ↗

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.Semantic proximity Read ↗

Structural Comparative Modeling of Multi-Domain F508del CFTR.Semantic proximity Read ↗

Structural comparative modeling of multi-domain ΔF508 CFTRSemantic proximity Read ↗

Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and StructureSemantic proximity Read ↗

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

Acting on the CFTR Membrane-Spanning Domains Interface Rescues Some Misfolded Mutants.Semantic proximity Read ↗

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

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

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.Semantic proximity Read ↗

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