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1 transferase and, likely, AICA ribonucleotide formyltransferase.
2 s similarity with glycinamide ribonucleotide formyltransferase.
3 is highly homologous to methionyl-tRNA(f)Met formyltransferase.
4 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase.
5 purine synthesis, glycinamide ribonucleotide formyltransferase.
6 ing purT (encoding phosphoribosylglycinamide formyltransferase 2 in the purine synthesis pathway) was
7 on aminoimidazole carboxamide ribonucleotide formyltransferase, 5,10-methylenetetrahydrofolate dehydr
8 ely the release of tetrahydrofolate from the formyltransferase active site or a conformational change
9                                 Although the formyltransferase activities of these proteins were far
10  aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), an enzyme in the purine bio
11 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), and thymidylate synthase (T
12 sting inhibition of both AICA ribonucleotide formyltransferase (AICARFTase) and glycinamide ribonucle
13 ls, aminoimidazolecarboxamide ribonucleotide formyltransferase (AICART), the second folate-dependent
14 is, aminoimidazolecarboxamide ribonucleotide formyltransferase (AICART).
15  iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin
16  fold as the related enzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formylt
17 zole carboxamide ribonucleotide, between the formyltransferase and the cyclohydrolase active sites.
18 ual inhibition of glycinamide ribonucleotide formyltransferase and, likely, AICA ribonucleotide formy
19 yltransferase and glycinamide ribonucleotide formyltransferase, but, unexpectedly, the structural sim
20 port the crystal structure of the N-terminal formyltransferase domain in a complex with uridine monop
21 ntity with Escherichia coli L-methionyl-tRNA formyltransferase (EC 2.1.2.9), was expressed as a solub
22 etrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2), an essential enzyme in d
23 hydrofolate dehydrogenase and methionyl-tRNA-formyltransferase extends to the C terminus of both prot
24                   In this study, we isolated formyltransferase (fmt) mutant strains of L. monocytogen
25 r gene encoding mitochondrial methionyl-tRNA formyltransferase (FMT1) has been deleted.
26 reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-aminoimidazole-4-carboxamid
27 uctase (DHFR) and glycinamide ribonucleotide formyltransferase (GARFT).
28 , suggesting that glycinamide ribonucleotide formyltransferase (GARFTase) in de novo purine biosynthe
29                   Glycinamide ribonucleotide formyltransferase (GARFTase) in R1-11-PCFT4 cells was in
30 e specificity and glycinamide ribonucleotide formyltransferase (GARFTase) inhibition.
31  (AICARFTase) and glycinamide ribonucleotide formyltransferase (GARFTase).
32 alogues inhibited glycinamide ribonucleotide formyltransferase (GARFTase).
33 e biosynthesis at glycinamide ribonucleotide formyltransferase (GARFTase).
34 ent inhibition of glycinamide ribonucleotide formyltransferase (GART) but do not induce detectable le
35 hetase (AIRS) and glycinamide ribonucleotide formyltransferase (GART) enzymatic activities.
36  created from the glycinamide-ribonucleotide formyltransferase (GART) genes from Escherichia coli (pu
37         The mouse glycinamide ribonucleotide formyltransferase (GART) locus is known to produce two f
38 ogs inhibitory to glycinamide ribonucleotide formyltransferase (GART).
39 fragment of human glycinamide ribonucleotide formyltransferase (hGART) was prepared and successfully
40 aminoimidazole- 4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (AICARFT/IMPCHase).
41 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a bifunctio
42 tein phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (PurH, EC 2.1.2.3/3
43 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase-mediated glucose tr
44 ent inhibitors of glycinamide ribonucleotide formyltransferase in de novo purine biosynthesis in KB h
45  and C2 inhibited glycinamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthe
46 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase (
47 locus, encoding mitochondrial methionyl-tRNA formyltransferase, lack detectable fMet-tRNAfMet but exh
48 e manner the Escherichia coli methionyl-tRNA formyltransferase (MTF) in the cytoplasm of the yeast Sa
49 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for initiation of p
50 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for initiation of p
51  methionyl-tRNA (Met-tRNA) by methionyl-tRNA formyltransferase (MTF) is important for the initiation
52 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation
53 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation
54 ionyl-tRNA (Met-tRNA(Met)) by methionyl-tRNA formyltransferase (MTF) is important for translation ini
55 tion reaction is catalyzed by methionyl-tRNA formyltransferase (MTF) located in mitochondria and uses
56 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF; EC 2.1.2.9) is important for the
57 n loop present in eubacterial methionyl-tRNA formyltransferases (MTF) is critical for specific recogn
58 sis of 10-formyl-THF, and the methionyl-tRNA formyltransferase (open reading frame YBL013W; designate
59 g aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, or IF2, we identified the steps limit
60       gart encodes phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase,
61  Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and the C-terminal fragment of
62  Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and, by genetic selection, iden
63 nt with significant in vivo flux through the formyltransferase reaction.
64 ifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) was studied by equilibrium d
65                   Glycinamide ribonucleotide formyltransferase was the principal cellular target.
66 nd in the E. coli glycinamide ribonucleotide formyltransferase, which, like MTF, use N(10)-formyltetr

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