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1 al corruption of translation, consumption of seryl-tRNA(Ala) by MurM may represent a first line of de
2 can incorporate seryl groups from mischarged Seryl-tRNA(Ala)(UGC) into cell wall precursors with exqu
3 s not present upstream of either copy of the seryl-tRNA(CAG) gene in eight other laboratory strains o
4 (which we designate beta) 9bp upstream of a seryl-tRNA(CAG) gene in the genome of Candida albicans.
6 e searched for unique structural features in seryl-tRNA(CAG), which translates the leucine CUG codon
9 nticodons are aminoacylated with serine, the seryl-tRNA is converted to selenocysteyl-tRNA and the la
11 ated that MJ0158 lacked affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and ne
12 se and demonstrated that the enzyme converts seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec) that could c
13 Bacterial selenocysteine synthase converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) for selenop
15 for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was directly conv
16 cifically phosphorylated the seryl moiety on seryl-tRNA[Ser]Sec and, in addition, had a requirement f
18 oding a flavin monooxygenase (vlmH, vlmR), a seryl tRNA synthetase gene (vlmL ) and seven genes of un
19 ryo-EM structures of the human mitochondrial seryl-tRNA synthetase (mSerRS) in complex with mtRNA(Ser
21 One example is the UNE-S domain, appended to seryl-tRNA synthetase (SerRS) in species that developed
22 cent studies suggested an essential role for seryl-tRNA synthetase (SerRS) in vascular development.
23 ix substrates revealed that Escherichia coli seryl-tRNA synthetase (SerRS) recognizes the 1--72 throu
25 utotrophicum contain a structurally uncommon seryl-tRNA synthetase (SerRS) sequence and lack an open
27 ires three steps: serylation of tRNA(Sec) by seryl-tRNA synthetase (SerRS), phosphorylation of Ser-tR
31 d-coil base provided by Thermus thermophilus seryl-tRNA synthetase and tested these chimeric construc
32 c) is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is
34 s SB-217452, has been found to be the active seryl-tRNA synthetase inhibitor component of albomycin d
36 ed protein that interacts with mitochondrial seryl-tRNA synthetase, as well as with mt-tRNAs containi
37 ass II enzymes, aspartyl-tRNA synthetase and seryl-tRNA synthetase, do not edit any of the amino acid
44 e Escherichia coli and Staphylococcus aureus seryl-tRNA synthetases in complex with aminoacyl adenyla
45 In contrast, both archaeal and bacterial seryl-tRNA synthetases were able to charge both archaeal
46 nhibitors that selectively inhibit bacterial seryl-tRNA synthetases with greater than 2 orders of mag
47 tRNA was found in rooster liver, and a minor seryl-tRNA that decoded the nonsense UGA was detected in
48 ivity that phosphorylated a minor species of seryl-tRNA to form phosphoseryl-tRNA was found in rooste
49 lyzes the transfer of the seryl residue from seryl-tRNA to the hydroxyl group of isobutylhydroxylamin
50 phosphoseryl-tRNA and the minor UGA-decoding seryl-tRNA were subsequently identified as selenocystein
51 mL in valanimycin biosynthesis is to produce seryl-tRNA, which is then utilized for a subsequent step