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1 A with cysteine by Methanococcus maripaludis cysteinyl-tRNA synthetase.
2 d evaluated as substrates for glutaminyl and cysteinyl-tRNA synthetases.
3 s are synthesized with comparable rates, the cysteinyl-tRNA synthetase activity being only 4.5-fold l
5 uggests similarities and differences between cysteinyl-tRNA synthetases and MshC in recognition of th
6 on factor 2, cell division protein FtsZ, and cysteinyl-tRNA synthetase as immunoreactive proteins.
7 hat, although the Escherichia coli and human cysteinyl-tRNA synthetases both recognize the same bases
11 for protein synthesis using both a canonical cysteinyl-tRNA synthetase (CysRS) as well as a set of tw
13 nd were used to identify a putative class II cysteinyl-tRNA synthetase (CysRS) in several archaea tha
14 ment of cysteine to tRNA(Cys) by the class I cysteinyl-tRNA synthetase (CysRS) is flexible; the enzym
16 t aminoacylation of tRNA by Escherichia coli cysteinyl-tRNA synthetase (CysRS) requires both domains,
17 that possess a canonical single-specificity cysteinyl-tRNA synthetase (CysRS), raising the question
22 that is unique to several halophile archaeal cysteinyl-tRNA synthetases (CysRS), which catalyze attac
23 synthetase (proS [mhp397]) (P = 0.009), and cysteinyl-tRNA synthetase (cysS [mhp661]) (P < 0.001) we
26 tion, the absence of a recognizable gene for cysteinyl tRNA synthetase in the genomes of Archae such
27 he cysS2 gene was thought to encode a second cysteinyl-tRNA synthetase in addition to cysS but the pr
30 association was also identified at the CARS (cysteinyl-tRNA synthetase) locus (OR = 1.36, P = 3.1 x 1
32 nnaschii possesses the unusual enzyme prolyl-cysteinyl-tRNA synthetase (ProCysRS), a single enzyme th
33 ions to the transit peptides of histidyl- or cysteinyl-tRNA synthetase, which are dual-targeted to ch
34 with phosphoserine (Sep), and the well known cysteinyl-tRNA synthetase, which charges the same tRNA w
35 tertiary fold of MshC is similar to that of cysteinyl-tRNA synthetase, with a Rossmann fold catalyti
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