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

Compounds that correct F508del-CFTR trafficking can also correct other protein trafficking diseases: an in vitro study using cell lines

14 Jan 2013

Abstract excerpt

BACKGROUND: Many genetic diseases are due to defects in protein trafficking where the mutant protein is recognized by the quality control systems, retained in the endoplasmic reticulum (ER), and degraded by the proteasome. In many cases, the mutant protein retains function if it can be trafficked to its proper cellular location. We have identified structurally diverse correctors that restore the trafficking and...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Genetics and Biotechnology
Share to Cellular transport and secretion
Share to Cystic Fibrosis Research Advances

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23316740
DOI: 10.1186/1750-1172-8-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Compounds that correct F508del-CFTR trafficking can also correct other protein trafficking diseases: an in vitro study using cell linesPMID 23316740Read ↗

G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo.Semantic proximity Read ↗

Correctors of the basic trafficking defect of the mutant F508del-CFTR that causes cystic fibrosis.Semantic proximity Read ↗

Rescue of vasopressin V2 receptor mutants by chemical chaperones: specificity and mechanism.Semantic proximity Read ↗

Rare Trafficking CFTR Mutations Involve Distinct Cellular Retention Machineries and Require Different Rescuing Strategies.Semantic proximity Read ↗

Analysis of the V2 Vasopressin Receptor (V2R) Mutations Causing Partial Nephrogenic Diabetes Insipidus Highlights a Sustainable Signaling by a Non-peptide V2R Agonist.Semantic proximity Read ↗

Corrector VX-809 stabilizes the first transmembrane domain of CFTR.Semantic proximity Read ↗

Pharmacological chaperones in nephrogenic diabetes insipidus: possibilities for clinical application.Semantic proximity Read ↗

A pharmacological chaperone stabilizer rescues the expression of the vast majority of pathogenic variants in a G protein-coupled receptorSemantic proximity Read ↗

Pharmacological Chaperones as Potential Therapeutic Strategies for Misfolded Mutant Vasopressin Receptors.Semantic proximity Read ↗

Targeting trafficking as a therapeutic avenue for misfolded GPCRs leading to endocrine diseases.Semantic proximity Read ↗

The rescue potentials of OPC-41061, OPC-31260 and OPC-21268 on mutant AVPR2s that cause nephrogenic diabetes insipidusSemantic proximity Read ↗

Small molecule correctors divert CFTR-F508del from ERAD by stabilizing sequential folding statesSemantic proximity Read ↗

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