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1 espectively), which both likely evolved from asparagine synthetase.
3 e inhibitor of the ammonia-dependent E. coli asparagine synthetase A (AS-A) can be regarded as such a
5 . possess asparagine-tRNA synthetase paralog asparagine synthetase A (LdASNA) that is ammonia-depende
8 acid is also a partial substrate for E. coli asparagine synthetase, acting as a nucleophile to form t
10 ndent asparagine formation in this bacterial asparagine synthetase and (ii) ammonia in bulk solution
11 (p-eIF2) leading to increased mRNA levels of asparagine synthetase and CCAAT/enhancer-binding protein
14 ion of the amino acid stress response genes, asparagine synthetase and CHOP/GADD153, increased as a r
15 We report the transactivation of two genes, asparagine synthetase and human telomerase reverse trans
16 ns genome of genes encoding tRNA-independent asparagine synthetase and the lack of this enzyme in D.
18 ative pentose pathway, malate dehydrogenase, asparagine synthetase, and histidine decarboxylase; and
20 o and in vitro characterizations of FdmV, an asparagine synthetase (AS) B-like protein, as an amide s
24 nd trans-factors affecting the expression of asparagine synthetase (AS) genes whose transcription is
25 ene for the amino acid biosynthetic activity asparagine synthetase (AS) is induced by both amino acid
27 f this family of ATP/Mg2+-dependent enzymes, asparagine synthetase (AS-B), catalyzes intermolecular,
28 AS1 and SAS2) encoding different isoforms of asparagine synthetase (AS; EC 6.3.5.4) were isolated.
30 clones, LJAS1 and LJAS2, encoding different asparagine synthetases (AS) have been identified and seq
32 genes such as glutamine synthetase (GLN) and asparagine synthetase (ASN) are modulated by carbon and
33 get genes involved in nitrogen assimilation: asparagine synthetase (ASN1 and ASN2) and glutamine synt
35 of ATF4 significantly reduced the levels of asparagine synthetase (ASNS) and overexpression of ASNS
39 er Genomic Atlas, and demonstrated that high asparagine synthetase (ASNS) expression correlated with
41 P suppressed the induction of the endogenous asparagine synthetase (ASNS) gene and inhibited transcri
42 stic leukemia (ALL), hypermethylation of the asparagine synthetase (ASNS) gene promoter, leading to l
43 ted analysis of these data revealed that the asparagine synthetase (ASNS) gene showed a gain in copy
44 of the cryo-EM map for wild-type (WT) human asparagine synthetase (ASNS) identifies a functional rol
45 oma model, we found that shRNA inhibition of asparagine synthetase (ASNS) or pharmacological inhibiti
48 ntigen 1 (FOSL1), transglutaminase 2 (TGM2), asparagine synthetase (ASNS), PLAB, PAOh1 and ELF3, whil
49 ion of ATF4 and the expression of its target asparagine synthetase (ASNS), sensitizing melanoma and p
52 he amino acid response induces expression of asparagine synthetase (ASNS), which provides for asparag
56 While ECs can take up asparagine, silencing asparagine synthetase (ASNS, which converts glutamine-de
57 ave examined the methylation profiles of the asparagine synthetase (ASY) promoter in a number of huma
58 mall-molecule inhibitors of Escherichia coli asparagine synthetase B (AS-B) as a model system for the
61 e aspartate binding site of Escherichia coli asparagine synthetase B (AS-B) using a number of stereoc
67 ragine synthetase A (AsnA), and the other is asparagine synthetase B (AsnB) that uses glutamine or am
68 osine (5'-FSBA) inactivates Escherichia coli asparagine synthetase B activity following pseudo-first-
70 in the synthetase active site of the enzyme asparagine synthetase B from Escherichia coli (AS-B).
72 nal architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for
73 s of the homologous primary metabolic enzyme asparagine synthetase B, and a chemical mechanism is pro
74 constitute a clinically useful inhibitor of asparagine synthetase B, these results suggested that re
78 other glutamine amidotransferases including asparagine synthetase, cytidine 5'-triphosphate (CTP) sy
81 rans and Thermus thermophilus do not possess asparagine synthetase (encoded by asnA or asnB), the enz
84 subfamily of amidotransferases that includes asparagine synthetase, glucosamine 6-phosphate synthase,
85 horibosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locatio
88 ted to increased HSC function as deletion of asparagine synthetase or treatment with 6-mercaptopurine
90 synthesis was suppressed, and expression of asparagine synthetase was statistically correlated with