![]() N-Asn structure
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Common Name | N-Asn | ||
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CAS Number | 2776-93-4 | Molecular Weight | 335.31000 | |
Density | 1.53g/cm3 | Boiling Point | 818.5ºC at 760mmHg | |
Molecular Formula | C12H21N3O8 | Melting Point | N/A | |
MSDS | Chinese USA | Flash Point | 448.8ºC |
Synthesis of N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine analogues. n-Butyramide, 3-chloropropionamide, 3-aminopropionamide, and isovaleramide analogues.
Carbohydr. Res. 331(4) , 439-44, (2001) The syntheses of four analogues of N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine are described. Activated carboxylic acids were reacted with 2-acetamido-2-deoxy-beta-D-glucopyranosylamine. n-Butyric anhydride gave N-(2-acetamido-2-deoxy-beta-D-g... |
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Aspartylglycosaminuria: biochemistry and molecular biology.
Biochim. Biophys. Acta 1455(2-3) , 139-54, (1999) Aspartylglucosaminuria (AGU, McKusick 208400) is an autosomal recessive lysosomal storage disease caused by defective degradation of Asn-linked glycoproteins. AGU mutations occur in the gene (AGA) for glycosylasparaginase, the enzyme necessary for hydrolysis ... |
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Angiokeratoma corporis diffusum in a Spanish patient with aspartylglucosaminuria.
Br. J. Dermatol. 147(4) , 760-4, (2002) Angiokeratoma corporis diffusum (ACD), initially considered to be synonymous with Fabry's disease, represents a well-known cutaneous marker of some other lysosomal enzyme disorders. Aspartylglucosaminuria (AGU) is a rare hereditary disorder mostly affecting t... |
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Bilateral pulvinar signal intensity decrease on T2-weighted images in patients with aspartylglucosaminuria.
Acta radiol. 49(6) , 687-92, (2008) Aspartylglucosaminuria (AGU) is an autosomal recessive lysosomal disease caused by deficiency of aspartylglucosaminidase. A thalamic T2 signal intensity decrease is associated with lysosomal diseases.To investigate thalamic signal intensity in AGU by performi... |
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Synthesis of an N-glucoasparagine analog as a building block for a V3-loop glycopeptide from gp120 of HIV-I.
Carbohydr. Res. 313(2) , 107-16, (1998) The preparative synthesis of a new N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine mimetic 1, starting from 2-amino-1,5-anhydro-2-deoxy-glucitol hydrochloride and Z-Asp-(OH)-OBn is described. This glycosyl-amino acid unit 1 is expected to show hig... |
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PCR-oligonucleotide ligation assay from dried blood spots.
Clin. Chem. 45(11) , 2022-5, (1999)
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Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Clin. Genet. 51(3) , 174-8, (1997) Aspartylglucosaminuria (AGU) is a lysosomal storage disease caused by deficiency of aspartylglucosaminidase. The disease is overrepresented in the Finnish population, in which one missense mutation (Cys163Ser) is responsible for 98% of the disease alleles. Th... |
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Sleep disturbances in aspartylglucosaminuria (AGU): a questionnaire study.
J. Inherit. Metab. Dis. 29(5) , 637-46, (2006) Sleep disturbances are common in many progressive metabolic encephalopathies. The possible presence of disturbed sleep-wake behaviour in the lysosomal storage disorder aspartylglucosaminuria, has not been previously studied, however. The sleep-wake behaviour ... |
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Phenotypic characterization of mice with targeted disruption of glycosylasparaginase gene: a mouse model for aspartylglycosaminuria.
J. Inherit. Metab. Dis. 21(3) , 207-9, (1998)
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Co-existence of lysosomal storage diseases in a consanguineous family.
Child Care. Health Dev. 27(2) , 173-81, (2001) Lysosomal storage diseases are rare and coexistence of more than one in a family can present a diagnostic challenge as illustrated by this study. The index case born to consanguineous Asian parents presented with developmental delay. Investigations led to an ... |