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Disease on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase

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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
amidase deficiency
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Anemia, Sickle Cell
Gardos pathway to sickle cell therapies?
Aspartylglucosaminuria
A fluorometric assay for glycosylasparaginase activity and detection of aspartylglycosaminuria.
A mouse model for the human lysosomal disease aspartylglycosaminuria.
A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase.
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Amlexanox provides a potential therapy for nonsense mutations in the lysosomal storage disorder Aspartylglucosaminuria.
Applications of a new fluorimetric enzyme assay for the diagnosis of aspartylglucosaminuria.
Aspartylglucosaminidase (AGA) is efficiently produced and endocytosed by glial cells: implication for the therapy of a lysosomal storage disorder.
Aspartylglucosaminuria (AGU): protein and gene structure of normal and mutated aspartylglucosaminidase.
Aspartylglucosaminuria among Palestinian Arabs.
Aspartylglucosaminuria caused by a novel homozygous mutation in the AGA gene was identified by an exome-first approach in a patient from Japan.
Aspartylglucosaminuria in a Canadian family.
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.
Aspartylglucosaminuria: deficiency of aspartylglucosaminidase in cultured fibroblasts of patients and their heterozygous parents.
Aspartylglucosaminuria: Unusual Neonatal Presentation in Qatari Twins With a Novel Aspartylglucosaminidase Gene Mutation and 3 New Cases in a Turkish Family.
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Assignment of the aspartylglucosaminidase gene (AGA) to 4q33----q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.
Bilateral pulvinar signal intensity decrease on T2-weighted images in patients with aspartylglucosaminuria.
Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.
Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.
Brain MRI findings in two Turkish pediatric patients with aspartylglucosaminuria.
Characterization of a point mutation in aspartylglucosaminidase gene: evidence for a readthrough of a translational stop codon.
Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.
Characterization of the storage material of peripheral lymphocytes in aspartylglycosaminuria.
Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.
Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.
Convenient and quantitative determination of the frequency of a mutant allele using solid-phase minisequencing: application to aspartylglucosaminuria in Finland.
Correction of deficient enzyme activity in a lysosomal storage disease, aspartylglucosaminuria, by enzyme replacement and retroviral gene transfer.
Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient.
Deletion of the 3'-untranslated region of aspartylglucosaminidase mRNA results in a lysosomal accumulation disease.
Deletion of the C-terminal end of aspartylglucosaminidase resulting in a lysosomal accumulation disease: evidence for a unique genomic rearrangement.
Dissection of the molecular consequences of a double mutation causing a human lysosomal disease.
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Enzymatic diagnosis of aspartylglycosaminuria by fluorometric assay of glycosylasparaginase in serum, plasma, or lymphocytes.
Enzyme replacement therapy in a mouse model of aspartylglycosaminuria.
Expression and endocytosis of lysosomal aspartylglucosaminidase in mouse primary neurons.
Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients.
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Genomic structure of human lysosomal glycosylasparaginase.
Glycoasparaginase in human urine.
Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts.
Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria.
Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.
Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria.
Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides.
Isolation of the liver N-aspartyl-beta-glucosaminidase in aspartylglucosaminuria.
Large-scale purification and preliminary x-ray diffraction studies of human aspartylglucosaminidase.
Large-scale purification of human aspartylglucosaminidase: utilization of exceptional sodium dodecyl sulfate resistance.
Linkage of aspartylglucosaminuria (AGU) to marker loci on the long arm of chromosome 4.
Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria.
Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.
Massive accumulation of Man2GlcNAc2-Asn in nonneuronal tissues of glycosylasparaginase-deficient mice and its removal by enzyme replacement therapy.
Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
Monitoring the CNS pathology in aspartylglucosaminuria mice.
Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuria.
Phenotypic characterization of mice with targeted disruption of glycosylasparaginase gene: a mouse model for aspartylglycosaminuria.
Pre-clinical Gene Therapy with AAV9/AGA in Aspartylglucosaminuria Mice Provides Evidence for Clinical Translation.
Progressive neurodegeneration in aspartylglycosaminuria mice.
Recombinant glycosylasparaginase and in vitro correction of aspartylglycosaminuria.
Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.
Single base deletion in exon 7 of the glycosylasparaginase gene causes a mild form of aspartylglycosaminuria in a patient of Mauritian origin.
Spectrum of mutations in aspartylglucosaminuria.
Splicing defect of the glycoasparaginase gene in two Japanese siblings with apartylglucosaminuria.
Structural basis of aspartylglucosaminuria.
Studies on N-aspartyl-beta-glucosaminidase in aspartylglycosaminuria.
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Toward understanding the neuronal pathogenesis of aspartylglucosaminuria: expression of aspartylglucosaminidase in brain during development.
Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Use of nonviral promoters in adenovirus-mediated gene therapy: reduction of lysosomal storage in the aspartylglucosaminuria mouse.
[Molecular analysis of the aspartylglucosaminidase gene in Japanese patients with aspartylglucosaminuria]
[Skeletal changes in 2 German children with aspartylglycosaminuria]
Congenital Disorders of Glycosylation
Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Cystic Fibrosis
Gene therapy to human diseases.
Genetic Diseases, Inborn
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Herpes Simplex
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Influenza, Human
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Intellectual Disability
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Toward understanding the neuronal pathogenesis of aspartylglucosaminuria: expression of aspartylglucosaminidase in brain during development.
Leukemia
Depletion of L-asparagine supply and apoptosis of leukemia cells induced by human glycosylasparaginase.
Lysosomal Storage Diseases
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.
Characterization of a point mutation in aspartylglucosaminidase gene: evidence for a readthrough of a translational stop codon.
Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.
Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.
Deletion of the 3'-untranslated region of aspartylglucosaminidase mRNA results in a lysosomal accumulation disease.
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Expression and endocytosis of lysosomal aspartylglucosaminidase in mouse primary neurons.
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Gene therapy to human diseases.
Genomic structure of human lysosomal glycosylasparaginase.
Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria.
Large-scale purification of human aspartylglucosaminidase: utilization of exceptional sodium dodecyl sulfate resistance.
Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients.
Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
Pre-clinical Gene Therapy with AAV9/AGA in Aspartylglucosaminuria Mice Provides Evidence for Clinical Translation.
Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.
Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Use of nonviral promoters in adenovirus-mediated gene therapy: reduction of lysosomal storage in the aspartylglucosaminuria mouse.
Mucolipidoses
Catabolism of N-glycosylprotein glycans: evidence for a degradation pathway of sialylglyco-asparagines resulting from the combined action of the lysosomal aspartylglucosaminidase and endo-N-acetyl-beta-D-glucosaminidase. A 400-MHz 1H-NMR study.
Glycosylasparaginase as a marker enzyme in the detection of I-cell disease
Glycosylasparaginase as a marker enzyme in the detection of I-cell disease.
n4-(beta-n-acetylglucosaminyl)-l-asparaginase deficiency
Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient.
Homozygous NADH-methemoglobin reductase and aspartylglucosaminidase deficiencies in a moderately retarded Sicilian child.
Splicing defect of the glycoasparaginase gene in two Japanese siblings with apartylglucosaminuria.
Parkinson Disease
Gene therapy to human diseases.
Rubella
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.