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 synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Jan 2005

Yam Gary Hin-Fai, Zuber Christian, Roth Jürgen

Abstract excerpt

Mutations in proteins that induce misfolding and proteasomal degradation are common causes of inherited diseases. Fabry disease is a lysosomal storage disorder caused by a deficiency of alpha-galactosidase A activity in lysosomes resulting in an accumulation of glycosphingolipid globotriosylceramide (Gb3). Some classical Fabry hemizygotes and all cardiac variants have residual alpha-galactosidase A activity, but...

Read the complete abstract on PubMed

Topics

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

Share to 1-Deoxynojirimycin
Share to alpha-Galactosidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arginine

Share to Fabry Disease

Share to Glutamine

Share to Lysosomes

Share to Molecular Chaperones

Share to Trihexosylceramides

Source

Identifiers

PMID: 15629890
DOI: 10.1096/fj.04-2375com

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 synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder.PMID 15629890Read ↗

Pharmacological chaperone therapy for Fabry disease.Semantic proximity Read ↗

Human α-Galactosidase A Mutants: Priceless Tools to Develop Novel Therapies for Fabry Disease.Semantic proximity Read ↗

Coformulation of a Novel Human α-Galactosidase A With the Pharmacological Chaperone AT1001 Leads to Improved Substrate Reduction in Fabry Mice.Semantic proximity Read ↗

Fabry disease: Mechanism and therapeutics strategiesSemantic proximity Read ↗

Candidate molecules for chemical chaperone therapy of GM1-gangliosidosis.Semantic proximity Read ↗

Emerging novel concept of chaperone therapies for protein misfolding diseases.Semantic proximity Read ↗

Beta-galactosidase deficiency: an approach to chaperone therapy.Semantic proximity Read ↗

Curcumin Has Beneficial Effects on Lysosomal Alpha-Galactosidase: Potential Implications for the Cure of Fabry Disease.Semantic proximity Read ↗

Progress and potential of non-inhibitory small molecule chaperones for the treatment of Gaucher disease and its implications for Parkinson disease.Semantic proximity Read ↗

Rescue of mutant alpha-galactosidase A in the endoplasmic reticulum by 1-deoxygalactonojirimycin leads to trafficking to lysosomes.Semantic proximity Read ↗

Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin.Semantic proximity Read ↗

Chaperone Therapy in Fabry Disease.Semantic proximity Read ↗

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