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 thermodynamic assay to test pharmacological chaperones for Fabry disease.

Biochimica et biophysica acta - 1 Mar 2014

Andreotti Giuseppina, Citro Valentina, Correra Antonella, Cubellis Maria Vittoria

Abstract excerpt

BACKGROUND: The majority of the disease-causing mutations affect protein stability, but not functional sites and are amenable, in principle, to be treated with pharmacological chaperones. These drugs enhance the thermodynamic stability of their targets. Fabry disease, a disorder caused by mutations in the gene encoding lysosomal alpha-galactosidase, represents an excellent model system to develop experimental...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Galactosidase
Share to Chlorocebus aethiops
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fabry Disease

Share to Molecular Chaperones

Share to Protein Stability

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 24361605
DOI: 10.1016/j.bbagen.2013.12.018
PMCID: PMC3909460

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 thermodynamic assay to test pharmacological chaperones for Fabry disease.PMID 24361605Read ↗

Prediction of the responsiveness to pharmacological chaperones: lysosomal human alpha-galactosidase, a case of study.Semantic proximity Read ↗

Identification of an Allosteric Binding Site on Human Lysosomal Alpha-Galactosidase Opens the Way to New Pharmacological Chaperones for Fabry Disease.Semantic proximity Read ↗

The New Pharmacological Chaperones PBXs Increase α-Galactosidase A Activity in Fabry Disease Cellular Models.Semantic proximity Read ↗

Taming molecular flexibility to tackle rare diseases.Semantic proximity Read ↗

A synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder.Semantic proximity Read ↗

Insights into human phosphoglycerate kinase 1 deficiency as a conformational disease from biochemical, biophysical, and in vitro expression analyses.Semantic proximity Read ↗

Treatment of Fabry's Disease with the Pharmacologic Chaperone Migalastat.Semantic proximity Read ↗

Protein structural features predict responsiveness to pharmacological chaperone treatment for three lysosomal storage disordersSemantic proximity Read ↗

Pharmacological chaperone therapy for Fabry disease.Semantic proximity Read ↗

Pharmacological chaperones: a new twist on receptor folding.Semantic proximity Read ↗

Drug Repositioning for Fabry Disease: Acetylsalicylic Acid Potentiates the Stabilization of Lysosomal Alpha-Galactosidase by Pharmacological Chaperones.Semantic proximity Read ↗

Cell-based screening of active-site specific chaperone for the treatment of Fabry disease.Semantic proximity Read ↗

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