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

doi:10.1038/mt.2015.87

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

Community

Back to search

Article

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

Molecular therapy : the journal of the American Society of Gene Therapy - 1 Jul 2015

Xu Su, Lun Yi, Brignol Nastry, Hamler Rick, Schilling Adriane, Frascella Michelle, Sullivan Sean, Boyd Robert E, Chang Kate, Soska Rebecca, Garcia Anadina, Feng Jessie, Yasukawa Hidehito, Shardlow Carole, Churchill Alison, Ketkar Amol, Robertson Nicola, Miyamoto Masahito, Mihara Kazutoshi, Benjamin Elfrida R, Lockhart David J, Hirato Tohru, Fowles Susie, Valenzano Kenneth J, Khanna Richie

Abstract excerpt

Fabry disease is an X-linked lysosomal storage disorder caused by mutations in the gene that encodes α-galactosidase A and is characterized by pathological accumulation of globotriaosylceramide and globotriaosylsphingosine. Earlier, the authors demonstrated that oral coadministration of the pharmacological chaperone AT1001 (migalastat HCl; 1-deoxygalactonojirimycin HCl) prior to intravenous administration of...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Galactosidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Combinations

Share to Enzyme Replacement Therapy

Share to Fabry Disease

Share to Fibroblasts

Share to Molecular Chaperones

Share to Oligopeptides

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 25915924
DOI: 10.1038/mt.2015.87
PMCID: PMC4817779

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coformulation of a Novel Human α-Galactosidase A With the Pharmacological Chaperone AT1001 Leads to Improved Substrate Reduction in Fabry Mice.PMID 25915924Read ↗

Pharmacological chaperone therapy for Fabry disease.Semantic proximity Read ↗

Developments in the treatment of Fabry disease.Semantic proximity Read ↗

Current and Investigational Therapeutics for Fabry DiseaseSemantic proximity Read ↗

Chaperone Therapy in Fabry Disease.Semantic proximity Read ↗

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

Safety and pharmacodynamic effects of a pharmacological chaperone on α-galactosidase A activity and globotriaosylceramide clearance in Fabry disease: report from two phase 2 clinical studiesSemantic proximity Read ↗

Fabry Disease Therapy: State-of-the-Art and Current ChallengesSemantic proximity Read ↗

Fabry disease: Mechanism and therapeutics strategiesSemantic proximity Read ↗

Enzyme replacement therapy for Fabry disease: lessons from two alpha-galactosidase A orphan products and one FDA approval.Semantic proximity Read ↗

Precision medicine in Fabry disease.Semantic proximity Read ↗

A review and recommendations for oral chaperone therapy in adult patients with Fabry disease.Semantic proximity Read ↗

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

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