ライフサイエンスコーパス: prolyl-tRNA synthetase

1 is not required for pre-transfer editing by prolyl-tRNA synthetase.

2 chii is an auxiliary function of a canonical prolyl-tRNA synthetase.

3 in corresponded to the predicted sequence of prolyl-tRNA synthetase.

4 c localization of the bifunctional glutamyl-/prolyl-tRNA synthetase.

5 d Ala-tRNA(Pro) that has been synthesized by prolyl-tRNA synthetase.

6 sion of a distinct isoform of bacterial-type prolyl-tRNA synthetase.

7 to the change in the recognition element for prolyl-tRNA-synthetase.

8 ory AKT signaling is coordinated by glutamyl-prolyl-tRNA synthetase 1 (EPRS1).

9 Our study reveals that the A culicifacies prolyl-tRNA synthetase (AcProRS) is potently inhibited b

10 tase activity being only 4.5-fold lower than prolyl-tRNA synthetase activity.

11 ), accuracy is difficult because the cognate prolyl-tRNA synthetase also recognizes and aminoacylates

12 Bacterial prolyl-tRNA synthetases and some smaller paralogs, YbaK

13 tionship between the evolutionary pattern of prolyl-tRNA synthetases and the emergence of two enzymat

14 Prolyl-tRNA synthetases are known to mischarge tRNA(Pro)

15 etase per amino acid, these organisms employ prolyl-tRNA synthetase as the enzyme that carries out Cy

16 NA synthetase and the bifunctional glutamyl-/prolyl-tRNA synthetase at the base of this asymmetric "V

17 nalyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRN

18 4444 C > A; p.Pro1482Thr), encoding glutamyl-prolyl-tRNA synthetase, consistent with HLD15.

19 we conclude that the evolutionary pattern of prolyl-tRNA synthetases does not obviously conform to th

20 s the catalytic glutamyl-tRNA synthetase and prolyl-tRNA synthetase domains.

21 A freestanding homologue of the prolyl-tRNA synthetase-editing domain, the PrdX protein

22 Specificity is dictated by glutamyl-prolyl tRNA synthetase (EPRS) binding to a 3'UTR element

23 gonist-inducible phosphorylation of glutamyl-prolyl tRNA synthetase (EPRS) by S6K1 in monocytes and a

24 Glutamyl-prolyl tRNA synthetase (EPRS) is a component of the hete

25 mportantly, the EN1-iPeps bound the glutamyl-prolyl tRNA synthetase (EPRS) target, which has been ass

26 entification of a truncated form of glutamyl-prolyl tRNA synthetase (EPRS), a GAIT constituent that m

27 te Ser(886) in the linker domain of glutamyl-prolyl tRNA synthetase (EPRS), the initial event in asse

28 Here we identify glutamyl-prolyl-tRNA synthetase (EPRS) as an mTORC1-S6K1 target t

29 ere we found that the MSC component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function foll

30 clinical compound that inhibits the glutamyl-prolyl-tRNA synthetase (EPRS) thereby inducing the integ

31 n EPRS1 gene encodes a bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) with two catalytic cores a

32 is heterotetrameric, consisting of glutamyl-prolyl-tRNA synthetase (EPRS), NS1-associated protein 1

33 Glutamyl-prolyl-tRNA synthetase (EPRS1) is a bifunctional aminoac

34 us spike protein, induce binding of glutamyl-prolyl-tRNA synthetase (EPRS1), within an unconventional

35 This study uses antibodies directed against prolyl-tRNA synthetase for immunoelectron microscopic lo

36 he pre-transfer editing activity of class II prolyl-tRNA synthetases from five species representing a

37 Translation of the glutamyl-prolyl-tRNA synthetase gene EPRS is enhanced in response

38 Here, we show that glutamyl-prolyl-tRNA synthetase (GluProRS), a bifunctional ARS of

39 a novel function of the fused glutamyl- and prolyl-tRNA synthetase (GluProRS).

40 years, aminoacyl-tRNA synthetases, including prolyl-tRNA synthetase, have emerged as attractive targe

41 The prolyl-tRNA synthetase inhibitor halofuginone blocks IL-

42 complexes, we develop a set of high-affinity prolyl-tRNA synthetase inhibitors, including previously

43 Additionally, we purified recombinant prolyl-tRNA synthetase of A culicifacies and performed e

44 It was reported that M. jannaschii prolyl-tRNA synthetase or the M. jannaschii MJ1477 prote

45 ain UQ818 with archaeal proS genes (encoding prolyl-tRNA synthetase) or with the Deinococcus radiodur

46 These data place the glutamyl-/prolyl-tRNA synthetase polypeptide in a defined area of

47 hermautotrophicus contain a dual-specificity prolyl-tRNA synthetase (ProCysRS) that accurately forms

48 Analysis of prolyl-tRNA synthetase (ProRS) across all three taxonomi

49 ermobacter thermautotrophicus proteins using prolyl-tRNA synthetase (ProRS) as the bait.

50 It has previously been proposed that the prolyl-tRNA synthetase (ProRS) enzymes in these organism

51 Class II prolyl-tRNA synthetase (ProRS) from Escherichia coli con

52 Using bacterial prolyl-tRNA synthetase (ProRS) genes as an example, we i

53 discrimination in the synthetic active site, prolyl-tRNA synthetase (ProRS) misactivates and mischarg

54 For the prolyl-tRNA synthetase (ProRS) of Methanococcus jannasch

55 Previous studies have shown that class II prolyl-tRNA synthetase (ProRS) possesses both pre- and p

56 Methanocaldococcus jannaschii prolyl-tRNA synthetase (ProRS) was previously reported t

57 eptor stem contacts made by Escherichia coli prolyl-tRNA synthetase (ProRS), an enzyme of unknown str

58 critical for recognition by Escherichia coli prolyl-tRNA synthetase (ProRS), but not for human ProRS.

59 Here we demonstrate that, for class II prolyl-tRNA synthetase (ProRS), functional coadaptations

60 dococcus jannaschii that was copurified with prolyl-tRNA synthetase (ProRS).

61 amblia indicated the presence of an archaeal prolyl-tRNA synthetase (ProRS).

62 ation into proteins due to misrecognition by prolyl-tRNA synthetase (ProRS).

63 Prolyl-tRNA synthetases (ProRS) have been shown to misac

64 Prolyl-tRNA synthetases (ProRS) mischarge tRNA(Pro) with

65 cific editing domain (INS) of most bacterial prolyl-tRNA synthetases (ProRSs) and an autonomous singl

66 Prolyl-tRNA synthetases (ProRSs) are notable due to thei

67 Prolyl-tRNA synthetases (ProRSs) can be divided into two

68 Prolyl-tRNA synthetases (ProRSs) from all three domains

69 Through primary sequence alignments, prolyl-tRNA synthetases (ProRSs) have been divided into

70 For example, prolyl-tRNA synthetases (ProRSs) mischarge alanine and c

71 One of these contained the prolyl tRNA synthetase (RS) gene.

72 insertion domain characteristic of bacterial prolyl-tRNA synthetase species, which is the site of pos

73 Inhibition of EPRS using a PRS (prolyl-tRNA synthetase)-specific inhibitor, halofuginone

74 establish a path for rational development of prolyl-tRNA synthetase-targeted anti-malarial therapies.

75 iting domain (INS) present in most bacterial prolyl-tRNA synthetases that hydrolyzes smaller Ala-tRNA

76 p biochemical assay for Plasmodium and human prolyl-tRNA synthetases that overcomes critical limitati

77 ansfer editing mechanism of Escherichia coli prolyl-tRNA synthetase was probed in detail.

78 ar, the entire set of available sequences of prolyl-tRNA synthetases was analyzed in this way.