PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20301412-8 1993 In mild/juvenile Canavan disease NAA may only be slightly elevated; thus, the diagnosis relies on molecular genetic testing of ASPA, the gene encoding the enzyme aspartoacylase. N-acetylaspartate 33-36 aspartoacylase Homo sapiens 127-131 33304759-1 2020 Canavan disease (CD) is a fatal leukodystrophy caused by mutation of the aspartoacylase (ASPA) gene, which leads to deficiency in ASPA activity, accumulation of the substrate N-acetyl-L-aspartate (NAA), demyelination, and spongy degeneration of the brain. N-acetylaspartate 175-195 aspartoacylase Homo sapiens 89-93 33304759-1 2020 Canavan disease (CD) is a fatal leukodystrophy caused by mutation of the aspartoacylase (ASPA) gene, which leads to deficiency in ASPA activity, accumulation of the substrate N-acetyl-L-aspartate (NAA), demyelination, and spongy degeneration of the brain. N-acetylaspartate 197-200 aspartoacylase Homo sapiens 89-93 27288788-3 2016 The physiological role of ASPA is to hydrolyse N-acetyl-l-aspartic acid (NAA), producing l-aspartic acid and acetate; as a result, its deficiency leads to abnormally high central nervous system NAA levels. N-acetylaspartate 47-71 aspartoacylase Homo sapiens 26-30 28879565-1 2017 Aspartoacylase (ASPA) is a zinc-dependent abundant enzyme in the brain, which catalyzes the conversion of N-acetyl aspartate (NAA) into acetate and aspartate. N-acetylaspartate 106-124 aspartoacylase Homo sapiens 0-14 28879565-1 2017 Aspartoacylase (ASPA) is a zinc-dependent abundant enzyme in the brain, which catalyzes the conversion of N-acetyl aspartate (NAA) into acetate and aspartate. N-acetylaspartate 106-124 aspartoacylase Homo sapiens 16-20 28879565-1 2017 Aspartoacylase (ASPA) is a zinc-dependent abundant enzyme in the brain, which catalyzes the conversion of N-acetyl aspartate (NAA) into acetate and aspartate. N-acetylaspartate 126-129 aspartoacylase Homo sapiens 0-14 28879565-1 2017 Aspartoacylase (ASPA) is a zinc-dependent abundant enzyme in the brain, which catalyzes the conversion of N-acetyl aspartate (NAA) into acetate and aspartate. N-acetylaspartate 126-129 aspartoacylase Homo sapiens 16-20 27531131-1 2017 Canavan disease (CD) is a rare fatal childhood neurological autosomal recessive genetic disease caused by mutations in the ASPA gene, which lead to catalytic deficiency of the ASPA enzyme, which catalyzes the hydrolysis of N-acetyl-L-aspartate (NAA) into aspartate and acetate. N-acetylaspartate 223-243 aspartoacylase Homo sapiens 123-127 27531131-1 2017 Canavan disease (CD) is a rare fatal childhood neurological autosomal recessive genetic disease caused by mutations in the ASPA gene, which lead to catalytic deficiency of the ASPA enzyme, which catalyzes the hydrolysis of N-acetyl-L-aspartate (NAA) into aspartate and acetate. N-acetylaspartate 223-243 aspartoacylase Homo sapiens 176-180 27531131-1 2017 Canavan disease (CD) is a rare fatal childhood neurological autosomal recessive genetic disease caused by mutations in the ASPA gene, which lead to catalytic deficiency of the ASPA enzyme, which catalyzes the hydrolysis of N-acetyl-L-aspartate (NAA) into aspartate and acetate. N-acetylaspartate 245-248 aspartoacylase Homo sapiens 123-127 27531131-1 2017 Canavan disease (CD) is a rare fatal childhood neurological autosomal recessive genetic disease caused by mutations in the ASPA gene, which lead to catalytic deficiency of the ASPA enzyme, which catalyzes the hydrolysis of N-acetyl-L-aspartate (NAA) into aspartate and acetate. N-acetylaspartate 245-248 aspartoacylase Homo sapiens 176-180 27288788-3 2016 The physiological role of ASPA is to hydrolyse N-acetyl-l-aspartic acid (NAA), producing l-aspartic acid and acetate; as a result, its deficiency leads to abnormally high central nervous system NAA levels. N-acetylaspartate 73-76 aspartoacylase Homo sapiens 26-30 27288788-3 2016 The physiological role of ASPA is to hydrolyse N-acetyl-l-aspartic acid (NAA), producing l-aspartic acid and acetate; as a result, its deficiency leads to abnormally high central nervous system NAA levels. N-acetylaspartate 194-197 aspartoacylase Homo sapiens 26-30 25573156-4 2015 N-acetyl-l-aspartate (NAA), the primary storage form of brain acetate, and aspartoacylase (ASPA), the enzyme responsible for NAA catalysis, are significantly reduced in GBM tumors. N-acetylaspartate 125-128 aspartoacylase Homo sapiens 91-95 26797702-1 2016 Aspartoacylase (ASPA) is an abundant enzyme in the brain, which catalyzes the conversion of N-acetylaspartate into acetate and aspartate, deficiency in its activity leads to degeneration of the white matter of the brain and is a recognized cause of Canavan disease (CD), which affect children. N-acetylaspartate 92-109 aspartoacylase Homo sapiens 0-14 26797702-1 2016 Aspartoacylase (ASPA) is an abundant enzyme in the brain, which catalyzes the conversion of N-acetylaspartate into acetate and aspartate, deficiency in its activity leads to degeneration of the white matter of the brain and is a recognized cause of Canavan disease (CD), which affect children. N-acetylaspartate 92-109 aspartoacylase Homo sapiens 16-20 26586007-8 2016 Classical elevation of NAA in brain and urine was present and genetic analysis identified mutations in the ASPA gene. N-acetylaspartate 23-26 aspartoacylase Homo sapiens 107-111 27089954-1 2016 The complete catalytic cycle of aspartoacylase (ASPA), a zinc-dependent enzyme responsible for cleavage of N-acetyl-l-aspartate, is characterized by the methods of molecular modeling. N-acetylaspartate 107-127 aspartoacylase Homo sapiens 32-46 27089954-1 2016 The complete catalytic cycle of aspartoacylase (ASPA), a zinc-dependent enzyme responsible for cleavage of N-acetyl-l-aspartate, is characterized by the methods of molecular modeling. N-acetylaspartate 107-127 aspartoacylase Homo sapiens 48-52 24278309-2 2013 N-acetyl-L-aspartate (NAA), the primary storage form of acetate in the brain, and aspartoacylase (ASPA), the enzyme responsible for NAA catalysis to generate acetate and ultimately acetyl-Coenzyme A for histone acetylation, are reduced in oligodendroglioma. N-acetylaspartate 132-135 aspartoacylase Homo sapiens 98-102 25189319-3 2015 NAA is catabolized by the enzyme aspartoacylase (ASPA) which is predominantly expressed in oligodendrocytes. N-acetylaspartate 0-3 aspartoacylase Homo sapiens 49-53 24977939-2 2014 CD is characterized by mutations in the gene encoding aspartoacylase (ASPA), the substrate enzyme that hydrolyzes N-acetylaspartic acid (NAA) to acetate and aspartate. N-acetylaspartate 114-135 aspartoacylase Homo sapiens 70-74 24977939-2 2014 CD is characterized by mutations in the gene encoding aspartoacylase (ASPA), the substrate enzyme that hydrolyzes N-acetylaspartic acid (NAA) to acetate and aspartate. N-acetylaspartate 137-140 aspartoacylase Homo sapiens 70-74 23996800-2 2014 Levels of N-acetyl-L-aspartate (NAA), the primary storage form of acetate in the brain, and aspartoacylase (ASPA), the enzyme responsible for NAA catalysis to generate acetate, are reduced in glioma; yet, few studies have investigated acetate as a potential therapeutic agent. N-acetylaspartate 142-145 aspartoacylase Homo sapiens 108-112 25003821-1 2014 Canavan disease (CD) is a fatal, childhood neurological disorder caused by mutations in the ASPA gene, leading to catalytic deficiencies in the aspartoacylase (ASPA) enzyme and impaired N-acetyl-l-aspartic acid metabolism in the brain. N-acetylaspartate 186-210 aspartoacylase Homo sapiens 92-96 22850825-2 2013 The enzyme aspartoacylase catalyzes the deacetylation of N-acetylaspartate to produce acetate required for fatty acid biosynthesis in the brain. N-acetylaspartate 57-74 aspartoacylase Homo sapiens 11-25 23884408-8 2013 Both NAA and NAAG elicited the expression of a novel immunoreactive ASPA species in select GSC nuclei, suggesting differential ASPA regulation in response to these metabolites. N-acetylaspartate 5-8 aspartoacylase Homo sapiens 68-72 23884408-8 2013 Both NAA and NAAG elicited the expression of a novel immunoreactive ASPA species in select GSC nuclei, suggesting differential ASPA regulation in response to these metabolites. N-acetylaspartate 5-8 aspartoacylase Homo sapiens 127-131 23151389-4 2013 Canavan disease (CD) is a globally occurring but rare early-onset human spongiform leukodystrophy associated with inborn genetic errors affecting the activity of aspartoacylase (ASPA), the enzyme highly expressed in oligodendrocytes that hydrolyzes NAA. N-acetylaspartate 249-252 aspartoacylase Homo sapiens 162-176 23151389-4 2013 Canavan disease (CD) is a globally occurring but rare early-onset human spongiform leukodystrophy associated with inborn genetic errors affecting the activity of aspartoacylase (ASPA), the enzyme highly expressed in oligodendrocytes that hydrolyzes NAA. N-acetylaspartate 249-252 aspartoacylase Homo sapiens 178-182 22468686-2 2012 The human aspartoacylase (ASPA) gene, which catalyzes the deacetylation of N-acetyl-L-aspartate, is mutated in Canavan disease. N-acetylaspartate 75-95 aspartoacylase Homo sapiens 10-24 23253610-1 2012 Canavan disease is a hereditary leukodystrophy caused by mutations in the aspartoacylase gene (ASPA), leading to loss of enzyme activity and increased concentrations of the substrate N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 183-201 aspartoacylase Homo sapiens 95-99 23253610-1 2012 Canavan disease is a hereditary leukodystrophy caused by mutations in the aspartoacylase gene (ASPA), leading to loss of enzyme activity and increased concentrations of the substrate N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 203-206 aspartoacylase Homo sapiens 95-99 23253610-8 2012 AAV2-ASPA gene therapy resulted in a decrease in elevated NAA in the brain and slowed progression of brain atrophy, with some improvement in seizure frequency and with stabilization of overall clinical status. N-acetylaspartate 58-61 aspartoacylase Homo sapiens 5-9 22468686-2 2012 The human aspartoacylase (ASPA) gene, which catalyzes the deacetylation of N-acetyl-L-aspartate, is mutated in Canavan disease. N-acetylaspartate 75-95 aspartoacylase Homo sapiens 26-30 16647192-2 2006 ASPA releases acetate by deacetylation of N-acetylaspartate (NAA), a highly abundant amino acid derivative in the central nervous system. N-acetylaspartate 42-59 aspartoacylase Homo sapiens 0-4 21474353-3 2011 CD is caused by mutations in the ASPA gene, which codes for the enzyme aspartoacylase (ASPA), which breaks down N-acetylaspartate (NAA) to acetate and aspartic acid. N-acetylaspartate 112-129 aspartoacylase Homo sapiens 33-37 21474353-3 2011 CD is caused by mutations in the ASPA gene, which codes for the enzyme aspartoacylase (ASPA), which breaks down N-acetylaspartate (NAA) to acetate and aspartic acid. N-acetylaspartate 112-129 aspartoacylase Homo sapiens 87-91 21474353-3 2011 CD is caused by mutations in the ASPA gene, which codes for the enzyme aspartoacylase (ASPA), which breaks down N-acetylaspartate (NAA) to acetate and aspartic acid. N-acetylaspartate 131-134 aspartoacylase Homo sapiens 33-37 21474353-3 2011 CD is caused by mutations in the ASPA gene, which codes for the enzyme aspartoacylase (ASPA), which breaks down N-acetylaspartate (NAA) to acetate and aspartic acid. N-acetylaspartate 131-134 aspartoacylase Homo sapiens 87-91 20673702-0 2010 Upregulation of N-acetylaspartic acid resulting nitric oxide toxicity induces aspartoacylase mutations and protein interaction to cause pathophysiology seen in Canavan disease. N-acetylaspartate 16-37 aspartoacylase Homo sapiens 78-92 20673702-1 2010 Aspartoacylase (ASPA) converts N-acetylaspartic acid into aspartate and acetate. N-acetylaspartate 31-52 aspartoacylase Homo sapiens 0-14 20673702-1 2010 Aspartoacylase (ASPA) converts N-acetylaspartic acid into aspartate and acetate. N-acetylaspartate 31-52 aspartoacylase Homo sapiens 16-20 20673702-2 2010 In Canavan disease (CD), N-acetylaspartic acid (NAA) is found to be increased and over 65 mutations including IVS4+1 G T, deletion of introns and exons have been reported in the ASPA gene. N-acetylaspartate 25-46 aspartoacylase Homo sapiens 180-184 20673702-2 2010 In Canavan disease (CD), N-acetylaspartic acid (NAA) is found to be increased and over 65 mutations including IVS4+1 G T, deletion of introns and exons have been reported in the ASPA gene. N-acetylaspartate 48-51 aspartoacylase Homo sapiens 180-184 20673702-7 2010 Therefore we hypothesize that upregulation of NAA stimulates NOS and the resulting nitric oxide toxicity induces ASPA mutations and protein interaction to result pathophysiological abnormalities seen in patients with CD. N-acetylaspartate 46-49 aspartoacylase Homo sapiens 113-117 19319678-5 2009 However, finding the links between the lacks of ASPA activity in oligodendrocytes, the buildup of NAA in white matter (WM) and the mechanisms underlying the edematous spongiform leukodystrophy have remained elusive. N-acetylaspartate 98-101 aspartoacylase Homo sapiens 48-52 17177147-1 2006 Canavan disease is a childhood leukodystrophy caused by mutations in the gene for human aspartoacylase ( ASPA), which leads to an abnormal accumulation of the substrate molecule N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 178-196 aspartoacylase Homo sapiens 88-102 17177147-1 2006 Canavan disease is a childhood leukodystrophy caused by mutations in the gene for human aspartoacylase ( ASPA), which leads to an abnormal accumulation of the substrate molecule N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 178-196 aspartoacylase Homo sapiens 105-109 17177147-1 2006 Canavan disease is a childhood leukodystrophy caused by mutations in the gene for human aspartoacylase ( ASPA), which leads to an abnormal accumulation of the substrate molecule N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 198-201 aspartoacylase Homo sapiens 88-102 17177147-1 2006 Canavan disease is a childhood leukodystrophy caused by mutations in the gene for human aspartoacylase ( ASPA), which leads to an abnormal accumulation of the substrate molecule N-acetyl-aspartate (NAA) in the brain. N-acetylaspartate 198-201 aspartoacylase Homo sapiens 105-109 22611636-2 2012 The deficiency of aspartoacylase (ASPA), resulting in the accumulation of N-acetyl aspartic acid (NAA) in the brain, plays an important role in the pathogenesis of the disease. N-acetylaspartate 74-96 aspartoacylase Homo sapiens 34-38 22611636-2 2012 The deficiency of aspartoacylase (ASPA), resulting in the accumulation of N-acetyl aspartic acid (NAA) in the brain, plays an important role in the pathogenesis of the disease. N-acetylaspartate 98-101 aspartoacylase Homo sapiens 34-38 17275978-3 2007 During early postnatal central nervous system (CNS) development, the expression of lipogenic enzymes in oligodendrocytes, including the NAA-degrading enzyme aspartoacylase (ASPA), is increased along with increased NAA production in neurons. N-acetylaspartate 136-139 aspartoacylase Homo sapiens 173-177 17275978-3 2007 During early postnatal central nervous system (CNS) development, the expression of lipogenic enzymes in oligodendrocytes, including the NAA-degrading enzyme aspartoacylase (ASPA), is increased along with increased NAA production in neurons. N-acetylaspartate 214-217 aspartoacylase Homo sapiens 173-177 17275978-4 2007 NAA is transported from neurons to the cytoplasm of oligodendrocytes, where ASPA cleaves the acetate moiety for use in fatty acid and steroid synthesis. N-acetylaspartate 0-3 aspartoacylase Homo sapiens 76-80 16647192-2 2006 ASPA releases acetate by deacetylation of N-acetylaspartate (NAA), a highly abundant amino acid derivative in the central nervous system. N-acetylaspartate 61-64 aspartoacylase Homo sapiens 0-4 16647192-5 2006 Our hypothesis is that ASPA actively participates in myelin synthesis by providing NAA-derived acetate for acetyl CoA synthesis, which in turn is used for synthesis of the lipid portion of myelin. N-acetylaspartate 83-86 aspartoacylase Homo sapiens 23-27 16802706-2 2006 Patients with CD have aspartoacylase (ASPA) deficiency, which results accumulation of N-acetylaspartic acid (NAA) in the brain and elevated excretion of urinary NAA. N-acetylaspartate 86-107 aspartoacylase Homo sapiens 38-42 16802706-2 2006 Patients with CD have aspartoacylase (ASPA) deficiency, which results accumulation of N-acetylaspartic acid (NAA) in the brain and elevated excretion of urinary NAA. N-acetylaspartate 109-112 aspartoacylase Homo sapiens 38-42 16802706-2 2006 Patients with CD have aspartoacylase (ASPA) deficiency, which results accumulation of N-acetylaspartic acid (NAA) in the brain and elevated excretion of urinary NAA. N-acetylaspartate 161-164 aspartoacylase Homo sapiens 38-42 35636725-2 2022 ASPA is highly expressed in oligodendrocytes and catalyzes the cleavage of N-acetylaspartate (NAA) to produce aspartate and acetate. N-acetylaspartate 75-92 aspartoacylase Homo sapiens 0-4 16807907-16 2006 ASPA gene delivery attempts in animal models have shown a lowering of N-acetyl L-aspartate and a change in motor functions, while sponginess of the WM, a characteristic of CD remained unchanged (Matalon et al. N-acetylaspartate 70-90 aspartoacylase Homo sapiens 0-4 10837925-7 2000 Our success in preparing the recombinant ASPA in high purity should permit multiple lines of investigations to understand the pathogenic mechanisms of Canavan disease and the functional roles of NAA. N-acetylaspartate 195-198 aspartoacylase Homo sapiens 41-45 16217711-4 2005 The altered NAA metabolism has been traced to mutations in the gene encoding ASPA, located on chromosome 17 (17p13-ter). N-acetylaspartate 12-15 aspartoacylase Homo sapiens 77-81 15784740-2 2005 ASPA acts to hydrolyze N-acetylaspartate (NAA) into l-aspartate and acetate, but the connection between ASPA deficiency and the failure of proper CNS development is unclear. N-acetylaspartate 23-40 aspartoacylase Homo sapiens 0-4 15784740-2 2005 ASPA acts to hydrolyze N-acetylaspartate (NAA) into l-aspartate and acetate, but the connection between ASPA deficiency and the failure of proper CNS development is unclear. N-acetylaspartate 42-45 aspartoacylase Homo sapiens 0-4 35636725-2 2022 ASPA is highly expressed in oligodendrocytes and catalyzes the cleavage of N-acetylaspartate (NAA) to produce aspartate and acetate. N-acetylaspartate 94-97 aspartoacylase Homo sapiens 0-4 35636725-3 2022 In this review ,we examine the pathologies and clinical presentation in CD, the metabolism and transportation of NAA in the brain, and the hypothetical mechanisms whereby ASPA deficiency results in dysmyelination and a failure of normal brain development. N-acetylaspartate 113-116 aspartoacylase Homo sapiens 171-175