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

A synonymous single nucleotide polymorphism in DeltaF508 CFTR alters the secondary structure of the mRNA and the expression of the mutant protein.

The Journal of biological chemistry - 10 Sept 2010

Bartoszewski Rafal A, Jablonsky Michael, Bartoszewska Sylwia, Stevenson Lauren, Dai Qun, Kappes John, Collawn James F, Bebok Zsuzsa

Abstract excerpt

Recent advances in our understanding of translational dynamics indicate that codon usage and mRNA secondary structure influence translation and protein folding. The most frequent cause of cystic fibrosis (CF) is the deletion of three nucleotides (CTT) from the cystic fibrosis transmembrane conductance regulator (CFTR) gene that includes the last cytosine (C) of isoleucine 507 (Ile507ATC) and the two thymidines...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Gene Expression Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HeLa Cells

Share to Models, Molecular

Share to Nucleic Acid Conformation

Share to Protein Folding

Share to RNA, Messenger

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 20628052
DOI: 10.1074/jbc.M110.154575
PMCID: PMC2937902

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

A synonymous single nucleotide polymorphism in DeltaF508 CFTR alters the secondary structure of the mRNA and the expression of the mutant protein.PMID 20628052Read ↗

The silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunction.Semantic proximity Read ↗

Features of CFTR mRNA and implications for therapeutics developmentSemantic proximity Read ↗

Codon bias and the folding dynamics of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

Functional analysis of synonymous substitutions predicted to affect splicing of the CFTR gene.Semantic proximity Read ↗

The Effect of Synonymous Single-Nucleotide Polymorphisms on an Atypical Cystic Fibrosis Clinical PresentationSemantic proximity Read ↗

Ribosomal frameshifting selectively modulates the assembly, function, and pharmacological rescue of a misfolded CFTR variant.Semantic proximity Read ↗

Alteration of protein function by a silent polymorphism linked to tRNA abundance.Semantic proximity Read ↗

Misfolding of the cystic fibrosis transmembrane conductance regulator and disease.Semantic proximity Read ↗

Disrupted post-transcriptional regulation of the cystic fibrosis transmembrane conductance regulator (CFTR) by a 5'UTR mutation is associated with a CFTR-related disease.Semantic proximity Read ↗

CFTR mRNA expression is regulated by an upstream open reading frame and RNA secondary structure in its 5' untranslated region.Semantic proximity Read ↗

Altered protein folding may be the molecular basis of most cases of cystic fibrosisSemantic proximity Read ↗

Synonymous codon usage affects the expression of wild type and F508del CFTR.Semantic proximity Read ↗

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