|1.||Mannosidase Deficiency Diseases (Mannosidosis)
|3.||Gaucher Disease (Gaucher's Disease)
|4.||Metachromatic Leukodystrophy (Sulfatide Lipidosis)
|5.||Globoid Cell Leukodystrophy (Krabbe Disease)
|1.||Jalanko, Anu: 3 articles (06/2006 - 06/2003)|
|2.||Mononen, Ilkka: 2 articles (10/2010 - 01/2005)|
|3.||Kelo, Eira: 2 articles (10/2010 - 01/2005)|
|4.||Dunder, Ulla: 2 articles (10/2010 - 01/2005)|
|5.||Laine, Minna: 2 articles (06/2006 - 06/2003)|
|6.||Laine, M: 2 articles (12/2004 - 04/2001)|
|7.||Jalanko, A: 2 articles (12/2004 - 04/2001)|
|8.||Mononen, I: 2 articles (06/2001 - 02/2000)|
|9.||Dunder, U: 2 articles (06/2001 - 02/2000)|
|10.||Sui, Lufei: 1 article (12/2014)|
07/15/2001 - "A deficiency, or absence, of enzyme activity gives rise to aspartylglycosaminuria, the most common disorder of glycoprotein metabolism. "
04/01/1996 - "Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation. "
03/01/1995 - "Aspartylglycosaminuria (AGU) is the most common disorder of glycoprotein degradation. "
10/01/1993 - "Aspartylglycosaminuria (AGU) (McKusick 20840) is the most common disorder of glycoprotein degradation caused by the failure of lysosomes to digest the protein-to-carbohydrate linkage of Asn-linked glycoproteins. "
10/01/1993 - "Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation."
05/30/1989 - "The sensitivity of the assay also allows direct quantitation of aspartylglucosamine in normal urine and leukocytes of aspartylglycosaminuria patients, and may thus be used in metabolic studies of the compound."
05/30/1989 - "The present method is applicable to the direct analysis of aspartylglucosamine in body fluids and tissues without any prepurification and, in combination with automated liquid chromatography, allows rapid assay of a large number of samples in the detection of aspartylglycosaminuria. "
03/15/1989 - "Aspartylglucosamine excretion in heterozygous carriers of aspartylglycosaminuria."
01/01/1988 - "As a conclusion, the determination of aspartylglucosamine in urine allowed postnatal detection of aspartylglycosaminuria, but in amniotic fluid it was useless in prenatal detection of the disease. "
01/01/1988 - "Aspartylglucosamine, the main metabolite accumulating in the body fluids and tissues in the disease, was measured with high-performance liquid chromatography in urine of aspartylglycosaminuria patients, carriers of the disease and normal controls as well as in amniotic fluid of normal pregnancies and one with the fetus affected by aspartylglycosaminuria. "
02/01/1972 - "Studies on serum and urinary glycopeptides and glycosaminoglycans in aspartylglucosaminuria."
03/15/1985 - "An abnormal excretion pattern of urinary glycosaminoglycans was found in patients with aspartylglycosaminuria, a lysosomal storage disorder of glycoprotein metabolism. "
03/15/1985 - "Urinary glycosaminoglycans in aspartylglycosaminuria: evidence for disturbed proteoglycan metabolism."
01/01/1987 - "The skin of the patients contained a normal amount and distribution of glycosaminoglycans, but the dermatan sulfate of aspartylglycosaminuria skin was more sensitive to chondroitinase AC digestion, resulting in unsaturated 4-sulfated disaccharides which were not detected in controls. "
01/01/1990 - "However, the activity of lysosomal enzymes, the excretion of mucopolysaccharides and oligosaccharides reactive to orcinol, as well as the search for aspartylglucosaminuria gave normal values. "
04/16/1975 - "Studies on N-aspartyl-beta-glucosaminidase in aspartylglycosaminuria."
03/10/1979 - "Two water-soluble glycoasparagine storage products were isolated from the liver of a patient with inherited deficiency of lysosomal N-aspartyl-beta-glucosaminidase (aspartylglycosaminuria). "
03/01/1976 - "The isolation of liver N-aspartyl-beta-glucosaminidase in human aspartylglucosaminuria, where this enzyme activity is diminished, yields an enzyme molecule with the same molecular weight and pH optimum as the normal enzyme. "
03/01/1976 - "Isolation of the liver N-aspartyl-beta-glucosaminidase in aspartylglucosaminuria."
01/01/2014 - "Biochemical investigations suggested aspartylglucosaminuria, and a novel homozygous mutation c.439T>C (p.S147P) was found in the aspartylglucosaminidase gene. "
01/01/2014 - "Aspartylglucosaminuria: unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family."
07/01/2008 - "Aspartylglucosaminuria (AGU) is an autosomal recessive lysosomal disease caused by deficiency of aspartylglucosaminidase. "
01/01/2005 - "Aspartylglycosaminuria (AGU) is caused by deficient enzymatic activity of glycosylasparaginase (GA). "
10/01/2004 - "A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase."
01/01/1988 - "The data demonstrate that the analysis of glycoasparagines in amniotic fluid is not likely to permit reliable prenatal diagnosis of aspartylglycosaminuria."
01/01/1988 - "Midterm amniotic fluid samples from one pregnancy with the fetus affected by aspartylglycosaminuria and from 11 normal pregnancies were analysed for glycoasparagines accumulating in urine in aspartylglycosaminuria. "
01/01/1988 - "Amniotic fluid glycoasparagines in fetal aspartylglycosaminuria."
03/10/1979 - "Accumulation of two glycoasparagines in the liver in aspartylglycosaminuria."
08/01/1976 - "Three different glycoasparagines have been isolated from the urine of a patient with aspartylglycosaminuria and their structures determined using sugar, amino acid and methylation analysis, enzymic degradation and measurements of the optical rotations. "
|8.||Neuraminidase deficiency with beta-galactosidase deficiencyIBA
11/01/2004 - "Lysosomal storage disorder samples include; aspartylglucosaminuria, galactosialidosis, Gaucher disease, GM1 gangliosidosis, mucopolysaccharidosis types I, II, IIIC, IVA, VI, and VII, mucolipidosis type II, multiple sulfatase deficiency, and sialidosis type II. Each disorder produced a unique signature metabolic profile of protein, oligosaccharide, and glycolipid markers. "
09/01/2013 - "We identified diagnostic urinary FOS patterns for α-mannosidosis, galactosialidosis, mucolipidosis type II/III, sialidosis, α-fucosidosis, aspartylglucosaminuria (AGU), Pompe disease, Gaucher disease, and GM1 and GM2 gangliosidosis. "
01/01/1990 - "This paper presents an overview of the biochemistry and the clinical spectrum of this group of diseases including sialidosis, galactosialidosis, alpha- and beta-mannosidosis, fucosidosis, aspartylglucosaminuria, and alpha-N-acetylgalactosaminidase deficiency (Schindler disease). "
01/01/2012 - "This method allows the detection of storage of oligosaccharides, which may indicate the presence of one of the infantile Pompe disease, α-mannosidosis, Gm1-gangliosidosis, Sandhoff disease, sialidosis, galactosialidosis, I-cell disease, and aspartylglucosaminuria."
09/01/1990 - "This method permits rapid screening and identification of disorders characterized by oligosacchariduria and glycopeptiduria including alpha-N-acetylgalactosaminidase deficiency, angiokeratoma corporis diffusum with glycopeptiduria, aspartylglucosaminuria, galactosialidosis, fucosidosis, GM1 gangliosidosis and sialidoses 1 and 2. Of note, the characterization of the glycopeptide excretion profiles in patients with alpha-N-acetylgalactosaminidase deficiency and angiokeratoma corporis diffusum with glycopeptiduria revealed essentially identical patterns, indicating the metabolic relatedness of these two phenotypically distinct conditions. "
01/01/1990 - "Elevated levels of serum dolichol in aspartylglucosaminuria."
06/01/1998 - "Two lysosomal storage diseases, aspartylglucosaminuria and mannosidosis, are associated with highly elevated serum dolichol concentrations. "
06/01/1992 - "Highly elevated serum total dolichol (free dolichol + dolichyl ester) concentrations have recently been found in two lysosomal storage diseases, aspartylglucosaminuria (AGU) and mannosidosis. "
12/01/1991 - "Our results suggest that serum dolichol concentration, which has earlier been found to be exceptionally high in aspartylglucosaminuria and mannosidosis, might serve as a laboratory marker for these recessively inherited lysosomal storage diseases."
01/01/1987 - "Changes in the structure and organization of collagen fibrils were recently described in the skin of aspartylglycosaminuria patients. "
01/01/1982 - "Aspartylglycosaminuria might thus provide a model for studying the regulation of collagen synthesis."
01/01/1982 - "Metabolism of collagen in aspartylglycosaminuria: decreased synthesis by cultured fibroblasts."
01/01/1987 - "This is indirect evidence for abnormal epimerization of dermatan sulfate in the skin of aspartylglycosaminuria patients, which may be associated with the changes in collagen fibril formation."
01/01/1984 - "Metabolism of collagen in aspartylglycosaminuria: urinary excretion of hydroxyproline."
|1.||Bone Marrow Transplantation (Transplantation, Bone Marrow)
12/01/2004 - "Bone marrow transplantation in young aspartylglucosaminuria mice: improved clearance of lysosomal storage in brain by using wild type as compared to heterozygote donors."
12/01/1999 - "Bone marrow transplantation in aspartylglucosaminuria--histopathological and MRI study."
02/01/2001 - "We cannot encourage bone marrow transplantation for the treatment of patients with aspartylglucosaminuria after infancy."
02/01/2001 - "Bone marrow transplantation for aspartylglucosaminuria: follow-up study of transplanted and non-transplanted patients."
09/01/1999 - "Correction of peripheral lysosomal accumulation in mice with aspartylglucosaminuria by bone marrow transplantation."
|2.||Enzyme Replacement Therapy
10/01/2010 - "Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice."
02/01/2000 - "Enzyme replacement therapy in a mouse model of aspartylglycosaminuria."
02/01/2000 - "These findings suggest that AGU may be correctable by enzyme therapy.-Dunder, U., Kaartinen, V., Valtonen, P., Väänänen, E., Kosma, V.-M., Heisterkamp, N., Groffen, J., Mononen, I. Enzyme replacement therapy in a mouse model of aspartylglycosaminuria."
|4.||Stem Cell Transplantation