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

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

Chemistry & biology - 1 Jan 2008

Pissarra Luísa S, Farinha Carlos M, Xu Zhe, Schmidt André, Thibodeau Patrick H, Cai Zhiwei, Thomas Philip J, Sheppard David N, Amaral Margarida D

Abstract excerpt

Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) Cl(-) channel. F508del, the most frequent CF-causing mutation, disrupts both the processing and function of CFTR. Recently, the crystal structure of the first nucleotide-binding domain of CFTR bearing F508del (F508del-NBD1) was elucidated. Although F508del-NBD1 shows only minor conformational changes relative to that...

Read the complete abstract on PubMed

Topics

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

Share to Crystallization
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cystic Fibrosis

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to Nucleotides

Share to Protein Conformation

Share to Solubility

Share to Stereoisomerism

Source

Identifiers

PMID: 18215773
DOI: 10.1016/j.chembiol.2007.11.012

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

Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation.PMID 18215773Read ↗

Defining the defect in F508 del CFTR: a soluble problem?Semantic proximity Read ↗

Rescue of Rare CFTR Trafficking Mutants Highlights a Structural Location-Dependent Pattern for Correction.Semantic 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 ↗

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

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 ↗

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

Structure basis of CFTR folding, function and pharmacology.Semantic proximity Read ↗

Nucleotide binding domains of human CFTR: a structural classification of critical residues and disease-causing mutations.Semantic proximity Read ↗

Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508.Semantic proximity Read ↗

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