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Accelerated transport and maturation of lysosomal α–galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
Fabry disease is a disorder of glycosphingolipid metabolism caused by deficiency of lysosomal α–galactosidase A (α–Gal A), resulting in renal failure along with premature myocardial infarction andExpand
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Alternative splicing in the alpha-galactosidase A gene: increased exon inclusion results in the Fabry cardiac phenotype.
Fabry disease is an inborn error of glycosphingolipid catabolism, resulting from deficient activity of lysosomal alpha-galactosidase A (alpha-Gal A). A rare alternative splicing that introduces aExpand
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Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by
Fabry disease is a lysosomal storage disorder caused by the deficiency of alpha-Gal A (alpha-galactosidase A) activity. In order to understand the molecular mechanism underlying alpha-Gal AExpand
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Transgenic mouse expressing human mutant alpha-galactosidase A in an endogenous enzyme deficient background: a biochemical animal model for studying active-site specific chaperone therapy for Fabry
Fabry disease is an inborn error of glycosphingolipid metabolism caused by the deficiency of lysosomal alpha-galactosidase A (alpha-Gal A). We have established transgenic mice that exclusivelyExpand
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Hydrophilic iminosugar active‐site‐specific chaperones increase residual glucocerebrosidase activity in fibroblasts from Gaucher patients
Gaucher disease is an autosomal recessive lysosomal storage disorder caused by the deficient activity of glucocerebrosidase. Accumulation of glucosylceramide, primarily in the lysosomes of cells ofExpand
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Preclinical Efficacy and Safety of 1-Deoxygalactonojirimycin in Mice for Fabry Disease
Fabry disease is an inborn error of glycosphingolipid metabolism caused by deficiency of α-galactosidase A (α-Gal A) activity. It has been shown that protein misfolding is primarily responsible forExpand
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Rescue of mutant alpha-galactosidase A in the endoplasmic reticulum by 1-deoxygalactonojirimycin leads to trafficking to lysosomes.
Active-site-specific chaperone therapy for Fabry disease is a genotype-specific therapy using a competitive inhibitor, 1-deoxygalactonojirimycin (DGJ). To elucidate the mechanism of enhancingExpand
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Efficient and rapid purification of recombinant human alpha-galactosidase A by affinity column chromatography.
The lysosomal enzyme alpha-galactosidase A (alpha-Gal A) metabolizes neutral glycosphingolipids that possess alpha-galactoside residues at the non-reducing terminus, and inherited defects in theExpand
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Introduction: Pharmacological chaperone therapy for lysosomal storage disorders – leveraging aspects of the folding pathway to maximize activity of misfolded mutant proteins
The initial protein-folding process is a thermodynamic equilibrium event. Despite the complexity of this process, there is ultimately only a small difference in energy that separates the properExpand
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