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1 (i) = 154 nM, IC(50) = 600 nM) against AICAR transformylase.
2 zyme of the purine biosynthesis pathway, GAR transformylase.
3 bservation that sulfasalazine inhibits AICAR transformylase.
4 an inhibitor of, glycinamide ribonucleotide transformylase.
5 trifunctional enzyme that also includes GAR transformylase.
6 ia coli and human glycinamide ribonucleotide transformylases.
7 -aminoimidazole-4-carboxamide ribonucleotide transformylase (347GG), methylenetetrahydrofolate reduct
8 parents targeted in earlier studies: two GAR transformylases (41% amino acid sequence identity), two
10 In yeast lacking MTHFS along with both AICAR transformylases, 5-CHO-THF was elevated 12-fold over wil
11 idazole-4-carboxamide ribonucleotide (AICAR) transformylase/5'-inosine monophosphate cyclohydrolase (
14 Identification of the location of the AICAR transformylase active site was previously elucidated fro
15 Potent and selective inhibition of the AICAR transformylase active site, compared with other folate-d
19 -aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase) is evaluated with pH depend
20 Aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase), one of the two folate-depe
22 aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase, residues 200-593)/IMPCH (AT
24 e synthetase, and glycinamide ribonucleotide transformylase, all of which have known three-dimensiona
25 e synthase (GARS), phosphoribosylglycinamide transformylase (also abbreviated as GART), and phosphori
26 midazole-4-carboxamidoribonucleotide (AICAR) transformylase, an enzyme involved in de novo purine bio
27 ithin de novo purine biosynthesis, the AICAR transformylase and IMP cyclohydrolase activities of the
29 unctional enzyme with folate-dependent AICAR transformylase and IMP cyclohydrolase activities that ca
30 vity of the bifunctional protein ATIC (AICAR transformylase and IMP cyclohydrolase) and is responsibl
31 -aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase
32 conservation around the active site of ArnA transformylase and other N-10-formyltetrahydrofolate-uti
33 erminal region of glycinamide ribonucleotide transformylase and several dinucleotide-dependent dehydr
34 -aminoimidazole-4-carboxamide ribonucleotide transformylase (ATIC) 347G were associated with methotre
35 dem repeats), amino imidazole ribonucleotide transformylase (ATIC) 347GG, and serine hydroxymethyltra
36 -aminoimidazole-4-carboxamide ribonucleotide transformylase (ATIC) and thymidylate synthase (TS).
37 sequence analyses, it is known that the PurT transformylase belongs to the ATP-grasp superfamily of p
38 to tetrahydrofolate and formate, whereas GAR transformylase catalyses the transfer of formyl from N10
39 osynthesis by MTX at the AICA ribonucleotide transformylase-catalyzed step may be related to the effi
40 amide ribonucleotide transformylase, or PurT transformylase, catalyzes an alternative formylation of
41 -resolution structural investigation of PurT transformylase complexed with various adenosine nucleoti
42 carboxyl-terminal region which, from the GAR transformylase crystal structure and labeling studies, i
45 AICAR is bound at the dimer interface of the transformylase domains and forms an extensive hydrogen b
46 timately bound at the dimer interface of the transformylase domains with the majority of AICAR moiety
49 cal to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2), resulted in the appearance
50 ycinamide ribonucleotide transformylase (GAR transformylase, EC 2.1.2.2) based on a steady-state and
53 on X-ray crystallographic structures of PurT transformylase from E. coli: one form complexed with the
54 analyses, it has been demonstrated that PurT transformylase from Escherichia coli belongs to the ATP-
55 amide ribonucleotide transformylase, or PurT transformylase, functions in purine biosynthesis by cata
60 rd purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) was monitored in live Escheri
61 hibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), which incorporate key featur
62 coli purT encoded glycinamide ribonucleotide transformylase (GAR transformylase) serves as an alterna
63 Escherichia coli glycinamide ribonucleotide transformylase (GAR transformylase, EC 2.1.2.2) based on
67 In animals, the phosphoribosylglycinamide transformylase (GART) gene encodes a trifunctional prote
69 Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) disrupts the observed pH-depen
70 ia coli and human glycinamide ribonucleotide transformylase genes, which have only 50% identity on th
72 me aminoimidazole-carboxamide ribonucleotide transformylase IMP cyclohydrolase, an enzyme not previou
73 idazole-4-carboxamide ribonucleotide (AICAR) transformylase/IMP cyclohydrolase (ATIC) is a bifunction
74 -Amino-4-imidazolecarboxamide ribonucleotide transformylase/IMP cyclohydrolase (ATIC) is a bifunction
77 me aminoimidazole carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATI
78 lase domain of the bifunctional enzyme AICAR transformylase/inosine monophosphate cyclohydrolase (ATI
79 -aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, Ste
80 -aminoimidazole-4-carboxamide ribonucleotide transformylase) is a folate-dependent activity of the bi
81 idazole-4-carboxamide ribonucleotide (AICAR) transformylase isozymes (ADE16 and ADE17) resulted in a
82 -aminoimidazole-4-carboxamide ribonucleotide transformylase isozymes that catalyze the penultimate st
83 the PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, catalyzes an alt
85 not formylated by the mitochondrial Met-tRNA transformylase preventing its function in initiation, an
87 e determined the equilibrium constant of the transformylase reaction to be 0.024 +/- 0.001, showing t
88 drolase and glycinamide ribonucleotide (GAR) transformylase, respectively, catalyze similiar yet dist
89 of lysyl-tRNA synthetase and methionyl-tRNA transformylase results in partial formylation of the mut
90 ycinamide ribonucleotide transformylase (GAR transformylase) serves as an alternate enzyme in the pro
92 hin 100- to 1000-fold of the native purN GAR transformylase validating the approach of constructing a