ASPA Antibody

1. report of 2 Egyptian sibling patients suspected of Canavan disease (CD); study revealed homozygosity for substitution T530C (Ile177Thr) in exon 4 of the ASPA gene in both sibs; substitution T530C (Ile177Thr) results in a novel missense mutation causing a CD phenotype with severe clinical characteristics PMID:24036223
2. Four ASPA missense mutations associated with Canavan disease are structurally characterized. PMID:25003821
3. Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein. PMID:24632142
4. This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent. PMID:22878930
5. a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease. PMID:22468686
6. Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver. PMID:22750302
7. Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis. PMID:22219087
8. We report on an Italian female patient with Canavan disease due to a missense mutation of the aspartoacylase gene and a 17p13.3 chromosomal microdeletion PMID:22019069
9. the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found PMID:12638939
10. Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene PMID:16437572
11. molecular weight of the purified enzyme is higher than predicted, suggesting the presence of post-translational modifications. Deglycosylation of aspartoacylase or mutation at glycosylation site causes decreased enzyme stability and catalytic activity PMID:16669630
12. a green fluorescent protein-human ASPA fusion protein larger than the permissible size for the nuclear pore complex was enzymatically active and showed mixed nuclear-cytoplasmic distribution. PMID:16935940
13. The finding that wild-type and Glu178Asp have the same K(m) but different k(cat) values confirms the idea that the carboxylate group contributes importantly to the enzymatic activity of aspartoacylase. PMID:17027983
14. the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A PMID:17194761
15. These results show that aspartoacylase is a member of the caboxypeptidase A family and offer novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease. PMID:17391648
16. New structure of human aspartoacylase complexed with a catalytic intermediate analogue, N-phosphonomethyl- l-aspartate, supports a carboxypeptidase-type mechanism for hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate. PMID:18293939

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HGNC: 756

UNIGENE: Hs.171142

KEGG: hsa:443

STRING: 9606.ENSP00000263080

OMIM: 271900