コーパス検索結果 (１語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 y direct nucleophilic attack by the amine of glycinamide ribonucleotide.
2 es ranging from 7.4 to 23.6 times the Km for glycinamide ribonucleotide.
3 alues ranged from 21 to 118 times the Km for glycinamide ribonucleotide.
4 Vmax values comparable to that obtained with glycinamide ribonucleotide, although the Km values range
7 0-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, hydroxyacetamide ri
8 ormyl dideazafolate and dideazafolate or for glycinamide ribonucleotide and formyl glycinamide ribonu
11 f GAR Tfase with its natural substrate, beta-glycinamide ribonucleotide (beta-GAR), at pH 8.5 confirm
14 ver, the O-phosphonate analog of carbocyclic glycinamide ribonucleotide did support enzymatic activit
15 ng the phosphonate derivative of carbocyclic glycinamide ribonucleotide, did not serve as substrates,
16 p of the purine biosynthetic pathway, formyl glycinamide ribonucleotide (FGAR) amidotransferase, also
18 cted against dihydrofolate reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-
19 including dihydrofolate reductase (DHFR) and glycinamide ribonucleotide formyltransferase (GARFT).
20 eceptor (FR) cellular uptake specificity and glycinamide ribonucleotide formyltransferase (GARFTase)
22 mino-4-imidazolecarboxamide, suggesting that glycinamide ribonucleotide formyltransferase (GARFTase)
24 of de novo purine nucleotide biosynthesis at glycinamide ribonucleotide formyltransferase (GARFTase).
25 ucleotide formyltransferase (AICARFTase) and glycinamide ribonucleotide formyltransferase (GARFTase).
26 ne synthesis because of potent inhibition of glycinamide ribonucleotide formyltransferase (GART) but
27 idazole ribonucleotide synthetase (AIRS) and glycinamide ribonucleotide formyltransferase (GART) enzy
29 ne synthesis by folate analogs inhibitory to glycinamide ribonucleotide formyltransferase (GART).
30 (PurN) and the C-terminal fragment of human glycinamide ribonucleotide formyltransferase (hGART) was
31 the N-terminal fragment of Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and
32 tested this methodology on Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and,
33 glutamate to recombinant trifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) w
34 ity was identified as the dual inhibition of glycinamide ribonucleotide formyltransferase and, likely
36 Compounds 7 and 11 were potent inhibitors of glycinamide ribonucleotide formyltransferase in de novo
38 nzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formyltransferase, but, unexp
39 l extension that is not found in the E. coli glycinamide ribonucleotide formyltransferase, which, lik
42 SCRATCHY libraries were created from the glycinamide-ribonucleotide formyltransferase (GART) gene
43 ase, catalyzes an alternative formylation of glycinamide ribonucleotide (GAR) in the de novo pathway
44 rN, N10-formyltetrahydrofolate hydrolase and glycinamide ribonucleotide (GAR) transformylase, respect
48 ism was implicated in which the enzyme binds glycinamide ribonucleotide or formyl dideazafolate produ
50 sylpyrophosphate amidotransferase (GPAT) and glycinamide ribonucleotide synthetase (GARS) from Aquife
51 re catalyzed by a trifunctional protein with glycinamide ribonucleotide synthetase (GARS), aminoimida
52 een prepared and evaluated as substrates for glycinamide ribonucleotide synthetase purified from chic
53 iosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism
54 tive site residues and loops in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).
55 esidue within 6 A of the catalytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).
60 lization pattern of the third purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) wa
61 Multisubstrate adduct inhibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), w
62 tic scheme is presented for Escherichia coli glycinamide ribonucleotide transformylase (GAR transform
65 ,6-diamino-4(3H)-oxopyrimidine inhibitors of glycinamide ribonucleotide transformylase (GART) are des
68 n in the dimer interface of Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) dis
69 shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several di
70 evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken l
71 fragments of the Escherichia coli and human glycinamide ribonucleotide transformylase genes, which h
72 minoimidazole ribonucleotide synthetase, and glycinamide ribonucleotide transformylase, all of which
76 03), which is 24-30% identical to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2),
79 nhibitors of the enzyme, competitive against glycinamide ribonucleotide, with Ki values ranging from
WebLSDに未収録の専門用語（用法）は "新規対訳" から投稿できます。