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 n reading frame (ylgG) specifying a putative Nudix hydrolase.
2 ATP activity is unique to MTH1 among related NUDIX hydrolases.
3 ties that were not consistent with the known Nudix hydrolases.
4 mary structure, unique among all other known Nudix hydrolases.
5 unctional, and evolutionary relationships to Nudix hydrolases.
6 and suggest a common catalytic mechanism for Nudix hydrolases.
7 s in thiopurine methyltransferase (TPMT) and Nudix hydrolase-15 (NUDT15) have been implicated as the
12 ase 1 (MTHFD1), we discovered a key role for Nudix hydrolase 5 (NUDT5) in regulating purine de novo s
13 Our study investigates the role of lncRNA Nudix Hydrolase 6 (NUDT6) and its antisense target fibro
19 and the purified protein was identified as a Nudix hydrolase active on FAD, adenosine 5'-triphospho-5
22 y characteristic of a family of enzymes, the Nudix hydrolases, active on a variety of nucleoside diph
23 of NrtR family having 2 unrelated functions (Nudix hydrolase and DNA binding), S. suis 2 retains a si
24 n to be associated with skin infections, the Nudix hydrolase and its associated genes may have a role
25 island-like emm region that included a novel Nudix hydrolase, and, further, this cluster appears to b
26 ther, contain a mutT motif characteristic of nudix hydrolases, and are conserved in all sequenced pox
30 mined the crystal structure, at 1.4A, of the Nudix hydrolase DR1025 from the extremely radiation resi
31 four structural superfamilies: MutT-related (Nudix) hydrolases, dUTPase, ITPase (Maf/HAM1) and all-al
33 vity and potential virulence function of the Nudix hydrolase effector AvrM14 from the flax rust fungu
34 t phosphate sensing by a conserved family of Nudix hydrolase effectors from pathogenic Magnaporthe an
35 indicate that some fungal pathogens produce Nudix hydrolase effectors with in vitro mRNA-decapping a
37 ide triphosphate pyrophophohydrolases of the Nudix hydrolase family discovered thus far, Orf135 is hi
45 The genome of Bacillus cereus contains 26 Nudix hydrolase genes, second only to its closest relati
47 th Mg2+, Zn2+, or Mn2+ and, like most of the Nudix hydrolases, has an alkaline pH optimum between 8.5
51 pporting the notion that the function of the Nudix hydrolases is to monitor the concentrations of rea
53 each subunit comprised of the ligand-binding Nudix hydrolase-like domain and the DNA-binding winged-h
54 des a decapping protein (ASFV-DP) that has a Nudix hydrolase motif and decapping activity in vitro He
55 decapping activity of D10 is dependent on a Nudix hydrolase motif that is also present in the VACV D
56 SFV) g5R gene encodes a protein containing a Nudix hydrolase motif which in terms of sequence appears
58 anel of human hydrolases and found that only Nudix hydrolase (NUDT) 18 catalyzed the hydrolysis of re
59 n mammalian cells and a role for DXO and the Nudix hydrolase Nudt12 in decapping NAD-capped RNAs (deN
61 cterization of a human cDNA encoding a novel nudix hydrolase NUDT5 for the hydrolysis of ADP-sugars.
62 specially difficult for the Escherichia coli Nudix hydrolase RppH, which triggers 5'-end-dependent RN
64 ocida encodes PnhA, which is a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
65 omogeneity and identified as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
66 eness of a human pathogen as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
67 ly been identified to encode a member of the Nudix hydrolase subfamily which acts specifically on din
68 oxynucleoside triphosphates or other typical Nudix hydrolase substrates, required a physiological lev
69 udA had hydrolytic activity typical of other Nudix hydrolases, such as Escherichia coli YgdP, in that
70 abundant 2,3-dehydratases that belong to the Nudix hydrolase superfamily and 3-dehydratases, which ar
72 k we have identified a new sub-family of the Nudix hydrolase superfamily recognizable by a specific a
73 e ytkD of Bacillus subtilis, a member of the Nudix hydrolase superfamily, has been cloned and express
74 A pyrophosphohydrolase RppH, a member of the Nudix hydrolase superfamily, triggers this degradation p
77 hosphatase NUDT9 belongs to a superfamily of Nudix hydrolases that catabolize potentially toxic compo
81 l-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecon
82 U" (where U is usually Leu, Val, or Ile) are Nudix hydrolases, which catalyze the hydrolysis of a var
83 sional structure of DR-CoAse, the first of a Nudix hydrolase with this specificity, reveals that this