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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
5 nthesis of a series of novel (4-alkoxyphenyl)glycinamides (e.g., 31) and the corresponding 1,3,4-oxad
6 both phenomena in a coordination compound of glycinamide (Glyam), [Ni(H(2)O)(2)(Glyam)(2)]I(2) (1).
7 th the tripeptide derivative glycine-proline-glycinamide in aqueous urea, aqueous TMAO, and aqueous u
10 and the reactivity of the simple nucleophile glycinamide is free of potential complications that aris
11 Analogues were studied where changes in the glycinamide moiety were combined with changes to the bas
13 f GAR Tfase with its natural substrate, beta-glycinamide ribonucleotide (beta-GAR), at pH 8.5 confirm
14 p of the purine biosynthetic pathway, formyl glycinamide ribonucleotide (FGAR) amidotransferase, also
15 ase, catalyzes an alternative formylation of glycinamide ribonucleotide (GAR) in the de novo pathway
16 rN, N10-formyltetrahydrofolate hydrolase and glycinamide ribonucleotide (GAR) transformylase, respect
20 0-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, hydroxyacetamide ri
21 ormyl dideazafolate and dideazafolate or for glycinamide ribonucleotide and formyl glycinamide ribonu
26 ver, the O-phosphonate analog of carbocyclic glycinamide ribonucleotide did support enzymatic activit
28 cted against dihydrofolate reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-
29 including dihydrofolate reductase (DHFR) and glycinamide ribonucleotide formyltransferase (GARFT).
31 mino-4-imidazolecarboxamide, suggesting that glycinamide ribonucleotide formyltransferase (GARFTase)
32 eceptor (FR) cellular uptake specificity and glycinamide ribonucleotide formyltransferase (GARFTase)
33 erine hydroxymethyl transferase (SHMT) 2 and glycinamide ribonucleotide formyltransferase (GARFTase)
35 of de novo purine nucleotide biosynthesis at glycinamide ribonucleotide formyltransferase (GARFTase).
36 ucleotide formyltransferase (AICARFTase) and glycinamide ribonucleotide formyltransferase (GARFTase).
37 ne synthesis because of potent inhibition of glycinamide ribonucleotide formyltransferase (GART) but
38 idazole ribonucleotide synthetase (AIRS) and glycinamide ribonucleotide formyltransferase (GART) enzy
40 ne synthesis by folate analogs inhibitory to glycinamide ribonucleotide formyltransferase (GART).
41 (PurN) and the C-terminal fragment of human glycinamide ribonucleotide formyltransferase (hGART) was
42 the N-terminal fragment of Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and
43 tested this methodology on Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and,
44 glutamate to recombinant trifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) w
45 ity was identified as the dual inhibition of glycinamide ribonucleotide formyltransferase and, likely
47 Compounds 7 and 11 were potent inhibitors of glycinamide ribonucleotide formyltransferase in de novo
49 nzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formyltransferase, but, unexp
50 l extension that is not found in the E. coli glycinamide ribonucleotide formyltransferase, which, lik
54 ism was implicated in which the enzyme binds glycinamide ribonucleotide or formyl dideazafolate produ
56 sylpyrophosphate amidotransferase (GPAT) and glycinamide ribonucleotide synthetase (GARS) from Aquife
57 re catalyzed by a trifunctional protein with glycinamide ribonucleotide synthetase (GARS), aminoimida
58 een prepared and evaluated as substrates for glycinamide ribonucleotide synthetase purified from chic
59 iosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism
60 tive site residues and loops in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).
61 esidue within 6 A of the catalytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).
66 lization pattern of the third purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) wa
67 Multisubstrate adduct inhibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), w
68 tic scheme is presented for Escherichia coli glycinamide ribonucleotide transformylase (GAR transform
71 ,6-diamino-4(3H)-oxopyrimidine inhibitors of glycinamide ribonucleotide transformylase (GART) are des
74 n in the dimer interface of Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) dis
75 shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several di
76 evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken l
77 fragments of the Escherichia coli and human glycinamide ribonucleotide transformylase genes, which h
78 minoimidazole ribonucleotide synthetase, and glycinamide ribonucleotide transformylase, all of which
82 03), which is 24-30% identical to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2),
85 Vmax values comparable to that obtained with glycinamide ribonucleotide, although the Km values range
86 ng the phosphonate derivative of carbocyclic glycinamide ribonucleotide, did not serve as substrates,
88 nhibitors of the enzyme, competitive against glycinamide ribonucleotide, with Ki values ranging from
92 SCRATCHY libraries were created from the glycinamide-ribonucleotide formyltransferase (GART) gene
96 ivatives by aldolization of pseudoephenamine glycinamide, which can be prepared from pseudoephenamine
97 At 25 degrees C, the uncatalyzed reaction of glycinamide with fPhe-TFE proceeds with a second-order r
98 lization of (R,R)- or (S,S)-pseudoephenamine glycinamide with lithium hexamethyldisilazide in the pre
99 within the ribosome, the reaction of aqueous glycinamide with N-formylphenylalanine trifluoroethyl es