ライフサイエンスコーパス: aspartoacylase

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1 effects of many missense mutations of human aspartoacylase.

2 partoacylase protein levels and undetectable aspartoacylase activity.

3 tures revealed that the N-terminal domain of aspartoacylase adopts a protein fold similar to that of

4 myosin-1d interacts and is co-expressed with aspartoacylase, an enzyme that plays a key role in fatty

5 oss of catalytic activity, thus establishing aspartoacylase as a zinc metalloenzyme.

6 It is demonstrated that aspartoacylase (ASP gene) and succinylglutamate desuccin

7 nked to mutations in the gene for the enzyme aspartoacylase (ASPA) (EC 3.5.1.15).

8 anavan disease is a leukodystrophy caused by aspartoacylase (ASPA) deficiency.

9 Aspartoacylase (ASPA) is an oligodendrocyte-restricted e

10 Recent studies have shown that aspartoacylase (ASPA), the defective enzyme in Canavan d

11 NAA and NAAG as well as aspartoacylase (ASPA), the enzyme responsible for NAA de

12 Mutations in the gene for aspartoacylase (ASPA), which catalyzes deacetylation of

13 ed perturbed metabolic regulators, including aspartoacylase (Aspa), which facilitates generation of a

14 ethal leukodystrophy caused by deficiency in aspartoacylase (ASPA), which hydrolyzes N-acetylaspartat

15 Aspartoacylase (ASPA)-deficient patients [Canavan diseas

16 (AAV)-based plasmids containing recombinant aspartoacylase (ASPA).

17 ve trait that is caused by the deficiency of aspartoacylase (ASPA).

18 Aspartoacylase (ASPA; EC 3.5.1.15) catalyzes deacetylati

19 tested a three-dimensional homology model of aspartoacylase based on zinc dependent carboxypeptidase

20 Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspart

21 Aspartoacylase catalyzes the deacetylation of N-acetylas

22 eviously shown to block brain vacuolation in aspartoacylase-deficient mice, also prevents neuron loss

23 About 100 C-terminal residues of aspartoacylase form a globular domain with a two-strande

24 The structure of human brain aspartoacylase has been determined in complex with a sta

25 Human aspartoacylase has now been successfully expressed in Pi

26 These results show that aspartoacylase is a member of the caboxypeptidase A fami

27 hypothesize that the catalytic mechanism of aspartoacylase is closely analogous to that of carboxype

28 novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease

29 avan disease is caused by inactivating ASPA (aspartoacylase) mutations that prevent cleavage of N-ace

30 Deglycosylation of aspartoacylase or mutation at the glycosylation site cau

31 (H21E/E24H and E24H/H116E) yielded wild-type aspartoacylase protein levels and undetectable ASPA acti

32 stabilization (R63N) also yielded wild-type aspartoacylase protein levels and undetectable aspartoac

33 y, and only E285A and P183H showed wild-type aspartoacylase protein levels.

34 stal structures of recombinant human and rat aspartoacylase refined to 2.8- and 1.8-A resolution, res

35 The catalytic site of aspartoacylase shows close structural similarity to thos

36 with the Escherichia coli-expressed form of aspartoacylase suggested the need for a suitable eukaryo

37 onserved substrate-determining residues with aspartoacylase that, when mutated, cause Canavan disease

38 malfunctioning of a single metabolic enzyme, aspartoacylase, that catalyzes the deacetylation of N-ac

39 that result in near undetectable activity of aspartoacylase, which catalyzes the deacetylation of N-a

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