| Aspartoacylase promotes the process of tumour development and is associated with immune infiltrates in gastric cancer. | Aspartoacylase promotes the process of tumour development and is associated with immune infiltrates in gastric cancer.
Han Y, Wang X, Xu M, Teng Z, Qin R, Tan G, Li P, Sun P, Liu H, Chen L, Jia B., Free PMC Article | 07/7/2023 |
| Mapping the degradation pathway of a disease-linked aspartoacylase variant. | Mapping the degradation pathway of a disease-linked aspartoacylase variant.
Gersing SK, Wang Y, Grønbæk-Thygesen M, Kampmeyer C, Clausen L, Willemoës M, Andréasson C, Stein A, Lindorff-Larsen K, Hartmann-Petersen R., Free PMC Article | 08/28/2021 |
| Allosteric Control of N-Acetyl-Aspartate Hydrolysis by the Y231C and F295S Mutants of Human Aspartoacylase | Allosteric Control of N-Acetyl-Aspartate Hydrolysis by the Y231C and F295S Mutants of Human Aspartoacylase.
Kots ED, Khrenova MG, Nemukhin AV. | 06/20/2020 |
| In one case, the homozygous pathogenic variant NM_000049.2:c.914C>A;p.Ala305Glu, which is previously reported in ClinVar, in the gene ASPA was identified causing Canavan disease. In the second case, the homozygous novel variant NM_000487.5:c.256C>G;p.Arg86Gly in the gene ARSA was identified causing metachromatic leukodystrophy. | First Record Mutations in the Genes ASPA and ARSA Causing Leukodystrophy in Jordan.
Froukh T., Free PMC Article | 06/15/2019 |
| 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 | New T530C mutation in the aspartoacylase gene caused Canavan disease with no correlation between severity and N-acetylaspartate excretion.
Di Pietro V, Cavallari U, Amorini AM, Lazzarino G, Longo S, Poggiani C, Cavalli P, Tavazzi B. | 10/18/2014 |
| Four ASPA missense mutations associated with Canavan disease are structurally characterized. | Aspartoacylase catalytic deficiency as the cause of Canavan disease: a structural perspective.
Wijayasinghe YS, Pavlovsky AG, Viola RE. | 09/27/2014 |
| Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein. | Reexamination of aspartoacylase: is this human enzyme really a glycoprotein?
Wang Q, Viola RE. | 05/31/2014 |
| This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent. | Molecular characterisation and prenatal diagnosis of Asparto-acylase deficiency (Canavan disease)--report of two novel and two known mutations from the Indian subcontinent.
Bijarnia S, Kohli S, Puri RD, Jacob RJ, Saxena R, Jalan A, Sistermans EA, Mahmood S, Verma IC. | 12/14/2013 |
| a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease. | A novel aspartoacylase (ASPA) gene mutation in Canavan disease.
Durmaz AA, Akin H, Onay H, Vahabi A, Ozkinay F. | 02/9/2013 |
| Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver. | Expression of aspartoacylase (ASPA) and Canavan disease.
Sommer A, Sass JO. | 10/13/2012 |
| Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis. | A missense mutation (p.G274R) in gene ASPA causes Canavan disease in a Pakistani family.
Hussain R, Daud S, Kakar N, Ahmad A, Baloch AH, Tareen AM, Kakar MA, Ahmad J. | 07/14/2012 |
| 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 | Chromosomal 17p13.3 microdeletion unmasking recessive Canavan disease mutation.
Cozzolino M, Augello B, Carella M, Palumbo O, Tavazzi B, Amorini AM, Lazzarino G, Merla G, Brunetti-Pierri N. | 03/17/2012 |
| Observational study and genome-wide association study of gene-disease association. (HuGE Navigator) | Human variation in alcohol response is influenced by variation in neuronal signaling genes.
Joslyn G, Ravindranathan A, Brush G, Schuckit M, White RL. | 04/7/2010 |
| 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. | Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue.
Le Coq J, Pavlovsky A, Malik R, Sanishvili R, Xu C, Viola RE., Free PMC Article | 01/21/2010 |
| Observational study of genotype prevalence. (HuGE Navigator) | See all PubMed (2) articlesCarrier frequency of autosomal-recessive disorders in the Ashkenazi Jewish population: should the rationale for mutation choice for screening be reevaluated?
Fares F, Badarneh K, Abosaleh M, Harari-Shaham A, Diukman R, David M. Canavan disease: carrier-frequency determination in the Ashkenazi Jewish population and development of a novel molecular diagnostic assay.
Feigenbaum A, Moore R, Clarke J, Hewson S, Chitayat D, Ray PN, Stockley TL. | 03/13/2008 |
| Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene | Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene.
Janson CG, Kolodny EH, Zeng BJ, Raghavan S, Pastores G, Torres P, Assadi M, McPhee S, Goldfarb O, Saslow B, Freese A, Wang DJ, Bilaniuk L, Shera D, Leone P. | 01/21/2010 |
| the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found | Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease.
Zeng BJ, Wang ZH, Ribeiro LA, Leone P, De Gasperi R, Kim SJ, Raghavan S, Ong E, Pastores GM, Kolodny EH. | 01/21/2010 |
| 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 | Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease.
Le Coq J, An HJ, Lebrilla C, Viola RE., Free PMC Article | 01/21/2010 |
| the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A | Structure of aspartoacylase, the brain enzyme impaired in Canavan disease.
Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr., Free PMC Article | 01/21/2010 |
| 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. | Mutational analysis of aspartoacylase: implications for Canavan disease.
Hershfield JR, Pattabiraman N, Madhavarao CN, Namboodiri MA., Free PMC Article | 01/21/2010 |
| 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. | Aspartoacylase is a regulated nuclear-cytoplasmic enzyme.
Hershfield JR, Madhavarao CN, Moffett JR, Benjamins JA, Garbern JY, Namboodiri A. | 01/21/2010 |
| 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. | Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease.
Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T. | 01/21/2010 |