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1                                              FPPS, a key branchpoint of the mevalonate pathway, catal
2  acids, converting the enzyme to an absolute FPPS by changing the cysteine to a tyrosine.
3 h the inhibitory activity of viperin against FPPS; indeed, some mutations potentiate viperin activity
4 rved amino acids that evolved from ancestral FPPSs and contribute to GPP/FPP product specificity.
5 e RcG/FPPS1 GPPS activity from the ancestral FPPSs, and shows that RcG/FPPS1 plays a key role in the
6 ophores for gammadelta T cell activation and FPPS inhibition both consisted of two negative ionizable
7 f the structural interaction between i6A and FPPS, pointing to i6A as a valuable lead compound in the
8 investigate the relationship between i6A and FPPS, we undertook an inverse virtual screening computat
9 ions between T. gondii growth inhibition and FPPS (human and Leishmania major) enzyme inhibition and
10 er human FPPS (HsFPPS) or Trypanosoma brucei FPPS (TbFPPS), the most active being the quinone methide
11 ally required for viperin to reduce cellular FPPS levels.
12 ertion present also in the Trypanosoma cruzi FPPS.
13 ules have high activity against an expressed FPPS from Leishmania major, in Dictyostelium discoideum
14  Escherichia coli showed enzyme activity for FPPS in vitro.
15 fields were quite similar to those found for FPPS inhibition by bisphosphonates.
16  gammadelta T cell activation with those for FPPS inhibition, using the Catalyst program.
17 gether with functional characterization of G/FPPS orthologs revealed that the G/FPPS activity is cons
18 tion of G/FPPS orthologs revealed that the G/FPPS activity is conserved among Rosaceae species.
19 icted hits had activity against either human FPPS (HsFPPS) or Trypanosoma brucei FPPS (TbFPPS), the m
20 he grouping of this enzyme with other type I FPPSs, but the biochemical data indicate that TgFPPS has
21 e highly correlated with their activities in FPPS inhibition: R = 0.88, p = 0.002, versus a human rec
22 n of FPPS but does not inhibit or inactivate FPPS.
23 ains found in polyprenyl synthases including FPPS, geranylgeranyl diphosphate synthases and hexapreny
24 C(50) for atovaquone (which does not inhibit FPPS) remained the same in the overexpressing strain.
25 mbrane, and it is thought that by inhibiting FPPS activity (and therefore cholesterol synthesis), vip
26  < 0.0001, for an expressed Leishmania major FPPS (N = 45 compounds).
27 ristics that differentiate it from mammalian FPPSs and GGPPSs and is therefore an important drug targ
28 es the intracellular rate of accumulation of FPPS but does not inhibit or inactivate FPPS.
29          The results identify new classes of FPPS inhibitors, diterpenoids and sesquiterpenoids, that
30 of substrate and bisphosphonate complexes of FPPS.
31 es, this cleavage reaction is independent of FPPS.
32 .77, p < 0.0001) and the final inhibition of FPPS by N-BPs ( R = 0.74, p < 0.0001) are closely linked
33 e molecular events involved in inhibition of FPPS by N-BPs, we used protein crystallography, enzyme k
34  NMR investigation of i6A in the presence of FPPS protein.
35       Several sequence motifs found in other FPPSs are present in TbFPPS, including an 11-mer peptide
36       Several sequence motifs found in other FPPSs are present in TcFPPS.
37 a T. gondii strain engineered to overexpress FPPS required considerably higher levels of bisphosphona
38                         However, some potent FPPS inhibitors had no activity in cell growth inhibitio
39 ing sites in both eukaryotic and prokaryotic FPPSs, in good accord with recent crystallographic resul
40  0.88, p = 0.002, versus a human recombinant FPPS (N = 9 compounds); R = 0.82, p < 0.0001, for an exp
41 ot act as a radical SAM enzyme in regulating FPPS.
42 Yet, the predicted enzyme sequences revealed FPPS motifs and homology with FPPS enzymes.
43 inhibition of farnesyl diphosphate synthase (FPPS) and geranylgeranyl diphosphate synthase (GGPPS), t
44               Farnesyl-diphosphate synthase (FPPS) catalyzes the synthesis of farnesyl diphosphate, a
45 ng studies of farnesyl diphosphate synthase (FPPS) inhibition, human Vgamma2Vdelta2 T cell activation
46 n and E. coli farnesyl diphosphate synthase (FPPS) inhibition.
47 ng the enzyme farnesyl diphosphate synthase (FPPS), but the details of how these molecules bind are n
48 thway enzymes farnesyl diphosphate synthase (FPPS), isopentenyl diphosphate/dimethylallyl diphosphate
49 teric site in farnesyl diphosphate synthase (FPPS).
50 thesis enzyme farnesyl diphosphate synthase (FPPS).
51 ncoding farnesyl diphosphate (FPP) synthase (FPPS) has been cloned from a cDNA library of Artemisia a
52 tion of the farnesyl pyrophosphate synthase (FPPS) activity.
53  osteoclast farnesyl pyrophosphate synthase (FPPS) and inhibit protein prenylation.
54  inhibiting farnesyl pyrophosphate synthase (FPPS) in osteoclasts, preventing protein prenylation.
55 ncoding the farnesyl pyrophosphate synthase (FPPS) of Trypanosoma brucei.
56 y inhibited farnesyl pyrophosphate synthase (FPPS) with IC50 values from 16 (alpha-F) to 340 (alpha-B
57 hway enzyme farnesyl pyrophosphate synthase (FPPS), as indicated by the correlations between T. gondi
58 hway enzyme farnesyl pyrophosphate synthase (FPPS), we also compared the pharmacophores for gammadelt
59 lar target, farnesyl pyrophosphate synthase (FPPS).
60   The corresponding synthases (FPP synthase [FPPS] and GGPP synthase [GGPPS]) catalyze, respectively,
61           Farnesyl pyrophosphate synthetase (FPPS) synthesizes farnesyl pyrophosphate through success
62 wed with antitumoral potential and targeting FPPS protein.
63                 These results establish that FPPS is essential for parasite viability and validate th
64  three isoprenoid diphosphates docked to the FPPS enzyme reveal strong electrostatic interactions wit
65                           In contrast to the FPPS of other eukaryotic organisms, TgFPPS is bifunction
66                              Together, these FPPS complexes provide a structural template for the des
67 rimetry, we show how these compounds bind to FPPS and/or GGPPS.
68  predict how several bisphosphonates bind to FPPS.
69 es, both as pure compounds and when bound to FPPS, to provide information about side-chain and phosph
70 a sequence of the cDNA was highly similar to FPPS from other plants, yeast and mammals, and contained
71 alpha-halo-analogues were ineffective versus FPPS (IC50 > 600 microM), but inhibited Rab geranylgeran
72 ences revealed FPPS motifs and homology with FPPS enzymes.