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1 was replaced with a more hydrophilic group, glycinamide.
3 f the pore volume became inaccessible to the glycinamide cation at the lowest ionic strength tested (
4 er scaffold modification to a (4-cyanophenyl)glycinamide (e.g., 29a) led to the development of compou
7 and the reactivity of the simple nucleophile glycinamide is free of potential complications that aris
8 Analogues were studied where changes in the glycinamide moiety were combined with changes to the bas
10 f GAR Tfase with its natural substrate, beta-glycinamide ribonucleotide (beta-GAR), at pH 8.5 confirm
11 p of the purine biosynthetic pathway, formyl glycinamide ribonucleotide (FGAR) amidotransferase, also
12 ase, catalyzes an alternative formylation of glycinamide ribonucleotide (GAR) in the de novo pathway
13 rN, N10-formyltetrahydrofolate hydrolase and glycinamide ribonucleotide (GAR) transformylase, respect
17 0-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, hydroxyacetamide ri
18 ormyl dideazafolate and dideazafolate or for glycinamide ribonucleotide and formyl glycinamide ribonu
23 ver, the O-phosphonate analog of carbocyclic glycinamide ribonucleotide did support enzymatic activit
25 cted against dihydrofolate reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-
26 including dihydrofolate reductase (DHFR) and glycinamide ribonucleotide formyltransferase (GARFT).
27 mino-4-imidazolecarboxamide, suggesting that glycinamide ribonucleotide formyltransferase (GARFTase)
28 eceptor (FR) cellular uptake specificity and glycinamide ribonucleotide formyltransferase (GARFTase)
31 of de novo purine nucleotide biosynthesis at glycinamide ribonucleotide formyltransferase (GARFTase).
32 ucleotide formyltransferase (AICARFTase) and glycinamide ribonucleotide formyltransferase (GARFTase).
33 ne synthesis because of potent inhibition of glycinamide ribonucleotide formyltransferase (GART) but
34 idazole ribonucleotide synthetase (AIRS) and glycinamide ribonucleotide formyltransferase (GART) enzy
36 ne synthesis by folate analogs inhibitory to glycinamide ribonucleotide formyltransferase (GART).
37 (PurN) and the C-terminal fragment of human glycinamide ribonucleotide formyltransferase (hGART) was
38 the N-terminal fragment of Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and
39 tested this methodology on Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and,
40 glutamate to recombinant trifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) w
41 ity was identified as the dual inhibition of glycinamide ribonucleotide formyltransferase and, likely
43 Compounds 7 and 11 were potent inhibitors of glycinamide ribonucleotide formyltransferase in de novo
45 nzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formyltransferase, but, unexp
46 l extension that is not found in the E. coli glycinamide ribonucleotide formyltransferase, which, lik
50 ism was implicated in which the enzyme binds glycinamide ribonucleotide or formyl dideazafolate produ
52 sylpyrophosphate amidotransferase (GPAT) and glycinamide ribonucleotide synthetase (GARS) from Aquife
53 re catalyzed by a trifunctional protein with glycinamide ribonucleotide synthetase (GARS), aminoimida
54 een prepared and evaluated as substrates for glycinamide ribonucleotide synthetase purified from chic
55 iosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism
56 tive site residues and loops in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).
57 esidue within 6 A of the catalytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).
62 lization pattern of the third purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) wa
63 Multisubstrate adduct inhibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), w
64 tic scheme is presented for Escherichia coli glycinamide ribonucleotide transformylase (GAR transform
67 ,6-diamino-4(3H)-oxopyrimidine inhibitors of glycinamide ribonucleotide transformylase (GART) are des
70 n in the dimer interface of Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) dis
71 shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several di
72 evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken l
73 fragments of the Escherichia coli and human glycinamide ribonucleotide transformylase genes, which h
74 minoimidazole ribonucleotide synthetase, and glycinamide ribonucleotide transformylase, all of which
78 03), which is 24-30% identical to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2),
81 Vmax values comparable to that obtained with glycinamide ribonucleotide, although the Km values range
82 ng the phosphonate derivative of carbocyclic glycinamide ribonucleotide, did not serve as substrates,
84 nhibitors of the enzyme, competitive against glycinamide ribonucleotide, with Ki values ranging from
88 SCRATCHY libraries were created from the glycinamide-ribonucleotide formyltransferase (GART) gene
91 ivatives by aldolization of pseudoephenamine glycinamide, which can be prepared from pseudoephenamine
92 At 25 degrees C, the uncatalyzed reaction of glycinamide with fPhe-TFE proceeds with a second-order r
93 lization of (R,R)- or (S,S)-pseudoephenamine glycinamide with lithium hexamethyldisilazide in the pre
94 within the ribosome, the reaction of aqueous glycinamide with N-formylphenylalanine trifluoroethyl es
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