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1  of the oligodendroglial NAA-cleaving enzyme aspartoacylase.
2  effects of many missense mutations of human aspartoacylase.
3 partoacylase protein levels and undetectable aspartoacylase activity.
4 tures revealed that the N-terminal domain of aspartoacylase adopts a protein fold similar to that of
5 myosin-1d interacts and is co-expressed with aspartoacylase, an enzyme that plays a key role in fatty
6 re leukodystrophy characterized by defective aspartoacylase and elevated N-acetyl-aspartic acid (NAA)
7 oss of catalytic activity, thus establishing aspartoacylase as a zinc metalloenzyme.
8                      It is demonstrated that aspartoacylase (ASP gene) and succinylglutamate desuccin
9 nked to mutations in the gene for the enzyme aspartoacylase (ASPA) (EC 3.5.1.15).
10 anavan disease is a leukodystrophy caused by aspartoacylase (ASPA) deficiency.
11                                              Aspartoacylase (ASPA) is an oligodendrocyte-restricted e
12               Recent studies have shown that aspartoacylase (ASPA), the defective enzyme in Canavan d
13                      NAA and NAAG as well as aspartoacylase (ASPA), the enzyme responsible for NAA de
14                    Mutations in the gene for aspartoacylase (ASPA), which catalyzes deacetylation of
15 ed perturbed metabolic regulators, including aspartoacylase (Aspa), which facilitates generation of a
16 ethal leukodystrophy caused by deficiency in aspartoacylase (ASPA), which hydrolyzes N-acetylaspartat
17                                              Aspartoacylase (ASPA)-deficient patients [Canavan diseas
18  (AAV)-based plasmids containing recombinant aspartoacylase (ASPA).
19 ve trait that is caused by the deficiency of aspartoacylase (ASPA).
20                                              Aspartoacylase (ASPA; EC 3.5.1.15) catalyzes deacetylati
21  present systematic studies of the cytosolic aspartoacylase, ASPA, where variants are linked to Canav
22 tested a three-dimensional homology model of aspartoacylase based on zinc dependent carboxypeptidase
23                                              Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspart
24                                              Aspartoacylase catalyzes the deacetylation of N-acetylas
25 cid antisense oligonucleotide to young-adult aspartoacylase-deficient mice reverses their pre-existin
26 eviously shown to block brain vacuolation in aspartoacylase-deficient mice, also prevents neuron loss
27             About 100 C-terminal residues of aspartoacylase form a globular domain with a two-strande
28                 The structure of human brain aspartoacylase has been determined in complex with a sta
29                                        Human aspartoacylase has now been successfully expressed in Pi
30                      These results show that aspartoacylase is a member of the caboxypeptidase A fami
31  hypothesize that the catalytic mechanism of aspartoacylase is closely analogous to that of carboxype
32 novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease
33 avan disease is caused by inactivating ASPA (aspartoacylase) mutations that prevent cleavage of N-ace
34                           Deglycosylation of aspartoacylase or mutation at the glycosylation site cau
35 (H21E/E24H and E24H/H116E) yielded wild-type aspartoacylase protein levels and undetectable ASPA acti
36  stabilization (R63N) also yielded wild-type aspartoacylase protein levels and undetectable aspartoac
37 y, and only E285A and P183H showed wild-type aspartoacylase protein levels.
38 stal structures of recombinant human and rat aspartoacylase refined to 2.8- and 1.8-A resolution, res
39                        The catalytic site of aspartoacylase shows close structural similarity to thos
40  with the Escherichia coli-expressed form of aspartoacylase suggested the need for a suitable eukaryo
41 onserved substrate-determining residues with aspartoacylase that, when mutated, cause Canavan disease
42 malfunctioning of a single metabolic enzyme, aspartoacylase, that catalyzes the deacetylation of N-ac
43 that result in near undetectable activity of aspartoacylase, which catalyzes the deacetylation of N-a